Information on EC 2.7.7.6 - DNA-directed RNA polymerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
2.7.7.6
-
RECOMMENDED NAME
GeneOntology No.
DNA-directed RNA polymerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nucleoside triphosphate + RNAn = diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
nucleoside triphosphate + RNAn = diphosphate + RNAn+1
show the reaction diagram
reaction mechanism
Q980R2, -
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
nucleotidyl group transfer
-
-
nucleotidyl group transfer
Pseudomonas putida WCS358
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Purine metabolism
-
Pyrimidine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C RNA formation factors
-
-
-
-
chloroplast soluble RNA polymerase
-
-
-
-
deoxyribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
-
DNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
DNA-dependent RNA nucleotidyltransferase
-
-
-
-
DNA-dependent RNA polymerase
-
-
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
Desulfurococcus mucosus 07
-
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
Q2WC24
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
P39466
-
DNA-dependent RNA polymerase
P46217, Q07271
-
DNA-dependent RNA polymerase
-
;
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
Thermoproteus tenax DSM 2078
-
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase
-
-
DNA-dependent RNA polymerase III
-
-
DNA-dependent RNA polymerases
-
-
DNA-dependent RNAP
Q2WC24
-
h-mtRNAP
-
-
K1E RNAP
Q2WC24
-
mitochondrial RNA polymerase
-
-
mitochondrial RNA polymerase
-
-
mitochondrial RNA polymerase
-
-
mtRNAP
Q2XSM7
-
multi-subunit RNA polymerase
-
-
multi-subunit RNA polymerase
B8YB53
-
multi-subunit RNA polymerase
B8YB53
-
-
multi-subunit RNA polymerase
-
-
nucleotidyltransferase, ribonucleate
-
-
-
-
Pol II
-
-
-
-
pol III
-
-
Pol IIIalpha
-
-
Pol IIIbeta
-
-
Pol IV
-
RNA polymerase complex
Pol V
-
RNA polymerase complex
ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleate polymerase
-
-
-
-
ribonucleic acid formation factors, C
-
-
-
-
ribonucleic acid nucleotidyltransferase
-
-
-
-
ribonucleic acid polymerase
-
-
-
-
ribonucleic acid transcriptase
-
-
-
-
ribonucleic polymerase
-
-
-
-
ribonucleic transcriptase
-
-
-
-
RNA formation factors, C
-
-
-
-
RNA nucleotidyltransferase
-
-
-
-
RNA nucleotidyltransferase (DNA-directed)
-
-
-
-
RNA pol III
-
-
RNA polymerase
-
-
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
Mycobacterium smegmatis mc2155
-
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
Pseudomonas putida WCS358
-
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
B2RFX8
-
RNA polymerase
-
-
RNA polymerase
-
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
B8YB53
-
RNA polymerase
B8YB53
-
-
RNA polymerase
-
-
RNA polymerase
D2SMJ0
-
RNA polymerase
D2SMK0
-
RNA polymerase
O08348, P0A0Y1, Q8PC55, Q8PC56
-
RNA polymerase core enzyme
-
-
RNA polymerase I
-
-
-
-
RNA polymerase I
-
-
RNA polymerase I
-
-
RNA polymerase I
-
-
RNA polymerase I
-
-
RNA polymerase II
-
-
-
-
RNA polymerase II
-
-
RNA polymerase II
-
-
RNA polymerase II
-
-
RNA polymerase II
-
-
RNA polymerase II
-
-
RNA polymerase II
P04050
-
RNA polymerase II
Saccharomyces cerevisiae yBC-10
-
-
-
RNA polymerase II
P36594
-
RNA polymerase II
Q980R2
-
RNA polymerase II
-
-
RNA polymerase II complex
-
-
RNA polymerase II complex
Leishmania major MHOM/IL/81/Friedlin
-
-
-
RNA polymerase III
-
-
-
-
RNA polymerase III
-
-
RNA polymerase III
-
-
RNA polymerase III complex
-
-
RNA polymerase III complex
Leishmania major MHOM/IL/81/Friedlin
-
-
-
RNA transcriptase
-
-
-
-
RNAP
-
-
-
-
RNAP
Mycobacterium smegmatis mc2155
-
-
-
RNAP
B8YB53
-
RNAP
B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64
-
RNAP
B8YB53
-
-
RNAP
B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64
;
-
RNAP core enzyme
-
-
RNAP I
-
-
-
-
RNAP II
-
-
-
-
RNAP II
-
consists of seven subunits: RPB1, RPB2, RPB3, RPB5, RPB7, RPB10, and RPB1
RNAP II
Leishmania major MHOM/IL/81/Friedlin
-
consists of seven subunits: RPB1, RPB2, RPB3, RPB5, RPB7, RPB10, and RPB1
-
RNAP II
Saccharomyces cerevisiae yBC-10
-
-
-
RNAP II
Q980R2
-
RNAP III
-
-
-
-
RNAP III
-
-
RNAP III
-
consists of subunits RPC1 (C160), RPC2 (C128), RPC3 (C82), RPC4 (C53), RPC5 (C37), RPC6 (C34), RPC9 (C17), RPAC1 (AC40), and RPAC2 (AC19)
RNAP III
Leishmania major MHOM/IL/81/Friedlin
-
consists of subunits RPC1 (C160), RPC2 (C128), RPC3 (C82), RPC4 (C53), RPC5 (C37), RPC6 (C34), RPC9 (C17), RPAC1 (AC40), and RPAC2 (AC19)
-
RNAP sigma70
-
-
RNAPII
-
-
rpo1N
B8YB53
gene name
rpo1N
B8YB53
gene name
-
Rpo41
-
gene name
RpoD
-
subunit D of RNA polymerase
RpoS
-
subunit sigma factor
RpoS
Pseudomonas putida WCS358
-
subunit sigma factor
-
Saci_0834
P39466
subunit E
sigma38 RNA polymerase
-
-
sigmaS-containing RNA polymerase
-
-
T7 RNA polymerase
-
-
T7 RNA polymerase
-
-
T7 RNAP
-
-
T7-like RNA polymerase
-
-
transcriptase
-
-
-
-
mitoRNAP
-
-
additional information
-
RNA polymerase is a member of the iron-sulfur cluster protein family
additional information
-
the enzyme belongs to the single-subunit, T7-like mitochondrial RNAP family
additional information
-
RNA polymerase is a member of the iron-sulfur cluster protein family
CAS REGISTRY NUMBER
COMMENTARY
9014-24-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
PCC 7120
-
-
Manually annotated by BRENDA team
Autographa californica M nucleopolyhedrovirus
-
-
-
Manually annotated by BRENDA team
RNA polymerase I, II and III
-
-
Manually annotated by BRENDA team
Desulfurococcus mucosus 07
-
-
-
Manually annotated by BRENDA team
several strains, gene rpoA
-
-
Manually annotated by BRENDA team
Fremyella diplosiphon
-
-
-
Manually annotated by BRENDA team
strain MHOM/IL/81/Friedlin
-
-
Manually annotated by BRENDA team
Leishmania major MHOM/IL/81/Friedlin
strain MHOM/IL/81/Friedlin
-
-
Manually annotated by BRENDA team
strain UR6
-
-
Manually annotated by BRENDA team
Leishmania sp. UR6
strain UR6
-
-
Manually annotated by BRENDA team
the nucleotide sequence of a part, 8334 bp, of the EcoRI fish lymphocystis disease virus DNA fragment B, between the EcoRI site and 259 nucleotides downstream from the second PstI site has been deposited in GenBank accession number: L34213
SwissProt
Manually annotated by BRENDA team
encoded on the linear mitochondrial plasmid
-
-
Manually annotated by BRENDA team
male C57Bl6 mice
-
-
Manually annotated by BRENDA team
strain mc2155
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis mc2155
strain mc2155
-
-
Manually annotated by BRENDA team
two RNA polymerase paralogues rpoB(S) and rpoB(R)
-
-
Manually annotated by BRENDA team
scorpionfly, collected in June in the village of Toksovo, Leningrad region, Russia
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
strain PAO1, ATCC 15692, and strain W1485
-
-
Manually annotated by BRENDA team
strain WCS358
-
-
Manually annotated by BRENDA team
Pseudomonas putida PpY101
PpY101
-
-
Manually annotated by BRENDA team
Pseudomonas putida WCS358
strain WCS358
-
-
Manually annotated by BRENDA team
strain yBC-10
-
-
Manually annotated by BRENDA team
strains YZS84 and YDP19
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae yBC-10
strain yBC-10
-
-
Manually annotated by BRENDA team
single phage-type RNA polymerase gene rpoT
UniProt
Manually annotated by BRENDA team
strain DSS12, a deep-sea piezophilic bacterium, genes rpoE2 and rpoE3
-
-
Manually annotated by BRENDA team
strain DSS12, a deep-sea piezophilic bacterium, genes rpoE2 and rpoE3
-
-
Manually annotated by BRENDA team
subunit L; strain DSM 639
SwissProt
Manually annotated by BRENDA team
subunit M; strain DSM 639
SwissProt
Manually annotated by BRENDA team
13-subunit enzyme
B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64
UniProt
Manually annotated by BRENDA team
13-subunit enzyme
B8YB53 and B8YB55 and B8YB54 and B8YB56 and B8YB57 and B8YB58 and B8YB59 and B8YB60 and B8YB61 and B8YB65 and B8YB62 and B8YB63 and B8YB64
UniProt
Manually annotated by BRENDA team
Thermoproteus tenax DSM 2078
-
-
-
Manually annotated by BRENDA team
procyclic, tsetse midgut wild-type form, Lister 427
-
-
Manually annotated by BRENDA team
strain WR
-
-
Manually annotated by BRENDA team
strain WR
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
UniProt
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
UniProt
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
gene rpoB encodes the RNA polymerase beta subunit
-
-
Manually annotated by BRENDA team
rpoA, alpha-subunit; pv. campestris
UniProt
Manually annotated by BRENDA team
rpoB; pv. campestris
UniProt
Manually annotated by BRENDA team
rpoC; pv. campestris
UniProt
Manually annotated by BRENDA team
rpoD; pv. campestris
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
human mitochondrial RNA polymerase is distantly related to the bacteriophage T7 class of single-subunit RNAPs with a probably similar mechanisms for nucleotide binding, substrate selection and catalysis/nucleotidyl transfer. The C-terminal domain contains the regions of highest similarity to the phage RNAPs. Early in the evolution of eukaryotes there has been a switch from a multi-subunit prokaryotic polymerase to a single-subunit, phage-derived polymerase, encoded in the nuclear genome and imported into the mitochondria, to serve as the transcriptase of the mitochondrial genome. The POLRMT CTD is characteristic of the Pol I family of nucleic acid polymerases, typically described as resembling the shape of a cupped right hand, containing the fingers, palm and thumb subdomains. The palm subdomain contains several key structural motifs that are highly conserved among the different classes of nucleic acid polymerases
evolution
-
Rpo41 utilizes a promoter recognition loop to bind and recognize its promoter, analogous to the use of the specificity loop by T7 RNAP for this purpose
malfunction
-
reverse translocation, i.e. backtracking, by a distance of one or more nucleotides disrupts the configuration of the catalytic center, leading to a temporary, spontaneously resolved, halt of the RNAP, called pausing, or to a transition into an irreversible arrested state. The latter can be restored to functionality by the endonucleolytic cleavage of the RNA or by pushing the backtracked complex from behind. Non-backtracked paused complexes are also described for bacterial RNAPs, where addition of the incoming NTP is hindered owing to isomerization of the active site into an inactive conformation
malfunction
-
DNA topoisomerase I inhibition by camptothecin induces escape of RNA polymerase II from promoter-proximal pause site, antisense transcription and histone acetylation at the human HIF-1alpha gene locus
malfunction
-
mutant Sc Rpb2 R512C is slow in elongation
malfunction
-
R428A RNAP is instable
malfunction
-
at lower concentrations, pyrimidine nucleoside analogs have the potential to more easily inhibit mitochondrial transcription and mediate toxicity, given the ability to be readily phosphorylated and serve as efficient substrates for the enzyme
malfunction
-
replication intermediates associated with an unusually prolonged delay in the initiation of second strand DNA synthesis are enhanced by combined shRNA and dsRNA POLRMT gene silencing
physiological function
-
Pol II is the eukaryotic enzyme that is responsible for transcribing all protein-coding genes into mRNA. The mRNA-transcription cycle can be divided into three stages: initiation, elongation and termination. During elongation, Pol II moves along a DNA template and synthesizes a complementary RNA chain in a processive manner
physiological function
-
detailed overview
physiological function
-
POLRMT is a key molecule of the core complex of the mitochondrial transcription machinery which assembles at promoter sequences on both strands of mtDNA, termed the L-strand promoter and H-strand promoter
physiological function
P04050
RNA polymerase II is the central enzyme of eukaryotic gene expression machinery, analysis of regulation mechanisms of transcription via protein-protein interactions within the Pol II apparatus, overview
physiological function
-
RNA pol III is involved in regulating the growth rate of cells
physiological function
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression
physiological function
-
RNAP-II is essential for gene expression in metazoa
physiological function
-
the enzyme from Zea mays exhibits a role in genome-wide and small RNA-associated gene silencing, but is not essential for the plant, PolIV is involved in paramutation, an inherited epigenetic change facilitated by an interaction of two alleles, overview
physiological function
-
the enzyme can be involved in both replication and integration processes of these plasmid in the mitochondrial genome
physiological function
-
RNA polymerase II has a regulatory function on nucleoside triphosphate synthesis, mutations of RNA polymerase II activate key genes of the nucleoside triphosphate biosynthetic pathways, overview
physiological function
-
the enzyme is required for expression of 13 subunits of the respiratory chain complexes involved in oxidative phosphorylation and two rRNAs and 22 tRNAs, required for mitochondrial translation. In addition to its role in transcription, in the mitochondria, POLRMT serves as the primase for mitochondrial DNA replication. Mechanisms and species specificity for promoter recognition, overview. Complex formation between the enzyme and the other transcription factors at the promoter, the structural elements of the enzyme are repositioned in such a way as to allow for specific promoter recognition, open complex formation and transcription initiation
physiological function
-
the enzyme is required for expression of 13 subunits of the respiratory chain complexes involved in oxidative phosphorylation and rRNAs and tRNAs, required for mitochondrial translation. Rpo41 can initiate transcription from negatively supercoiled templates and pre-melted promoter substrates in the absence of the yeast mitochondrial transcription factor, Mtf1. Mechanisms and species specificity for promoter recognition, overview
physiological function
-
mitochondrial DNA is replicated by a unique enzymatic machinery involving the POLRMT-mediated initiation of primer synthesis from a poly-dT stretch in the single-stranded loop region of the light-strand origin of DNA replication, when the single-stranded origin of DNA replication is exposed and adopts a stem-loop structure. The poly-dT repeat region of origin of DNA replication is an essential element for primer synthesis. POLRMT can function as an origin-specific primase in mammalian mitochondria, overview
physiological function
-
the enzyme activates genes for high affinity nutrient scavenging and motility
physiological function
-
increased Pol III transcription accompanies or causes cell transformation. RPC32beta subunit-containing isozyme Pol IIIbeta is ubiquitously expressed and essential for growth of human cells. RPC32alpha subunit-containing isozyme Pol IIIalpha is dispensable for cell survival, with expression being restricted to undifferentiated ES cells and to tumor cells. Dramatic changes in 5S RNA, U6 RNA, and 7SKRNA expression are specifically caused by ectopic expression of RPC32alpha and not due to a general deregulation of transcription
malfunction
-
suppression of subunit RPC32alpha expression by siRNAs impedes anchorage-independent growth of HeLa cells, whereas ectopic expression of RPC32alpha in IMR90 fibroblasts enhances cell transformation and dramatically changes the expression of several tumor-related mRNAs and that of a subset of Pol III RNAs
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
in vitro assembly of Sc RNAP II ternary elongation complexes, overview. RNA polymerase in a catalytic conformation demonstrates that the active site dNMP-NTP base pair must be substantially dehydrated to support full active site closing and optimum conditions for phosphodiester bond synthesis. An active site latch assembly that includes a key trigger helix residue beta' H1242 and highly conserved active site residues beta E445 and R557 appears to help regulate active site hydration/dehydration. Molecular dynamics simulations, overview
additional information
-
modeling of Tt RNAP TEC containing a closed, catalytic trigger helix conformation. RNA polymerase in a catalytic conformation demonstrates that the active site dNMP-NTP base pair must be substantially dehydrated to support full active site closing and optimum conditions for phosphodiester bond synthesis. An active site latch assembly that includes a key trigger helix residue beta' H1242 and highly conserved active site residues beta E445 and R557 appears to help regulate active site hydration/dehydration. Molecular dynamics simulations, overview
additional information
-
POLRMT distinct mechanisms for promoter recognition and transcription initiation, kinetic mechanism for POLRMT-catalyzed nucleotide incorporation, and structure-function relationship, nucleotidyl transfer and the nucleotide-addition cycle, detailed overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-C-methyl-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
misincorporation frequency of approximately 1 in 7800 2'-C-methyl-ATP
-
-
?
2'-deoxy-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
misincorporation
-
-
?
3'-deoxy-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
misincorporation frequency of approximately 1 in 5 3'-dATP
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
d(Ap4T) + RNAn
?
show the reaction diagram
-
primer elongation
-
-
?
d(TP4C) + RNAn
?
show the reaction diagram
-
primer elongation
-
-
?
d(Tp4G) + RNAn
?
show the reaction diagram
-
primer elongation
-
-
?
d(Tp4T) + RNAn
?
show the reaction diagram
-
primer elongation
-
-
?
DNA + 5-[[(2-aminoethyl)amino]carbonyl]-UTP
?
show the reaction diagram
-
-
-
-
?
DNA + 5-[[(2-methylpropyl)amino]carbonyl]-UTP
?
show the reaction diagram
-
-
-
-
?
DNA + 5-[[(2-pyridinylmethyl)amino]carbonyl]-UTP
?
show the reaction diagram
-
-
-
-
?
DNA + 5-[[(4-pyridinylmethyl)amino]carbonyl]-UTP
?
show the reaction diagram
-
-
-
-
?
DNA + 5-[[benzylamino]carbonyl]-UTP
?
show the reaction diagram
-
-
-
-
?
DNA + 5-[[[2-(1H-imidazol-4-yl)ethyl]amino]carbonyl]-UTP
?
show the reaction diagram
-
-
-
-
?
DNA + 5-[[[2-(1H-indol-3-yl)ethyl]amino]carbonyl]-UTP
?
show the reaction diagram
-
-
-
-
?
dTTP + RNAn
?
show the reaction diagram
-
primer elongation
-
-
?
GTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + A10G2A2C2C
?
show the reaction diagram
-
oligonucleotide extension
-
-
?
nucleoside triphosphate + A9G3A2C2C
?
show the reaction diagram
-
oligonucleotide extension
-
-
?
nucleoside triphosphate + G2CAC2C
?
show the reaction diagram
-
oligonucleotide extension
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, Q2XSM7
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q980R2, -
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme can bind to DNA containing the lambdaPR promoter, form an open complex and initiate transcription in a temperature-dependent manner. The organism relies on the high temperature of its environment to provide the thermal energy required to stimulate open promoter complex formation, initiate transcription, and facilitate the conformational changes in RNA polymerase that results in nucleotide incorporation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
calf thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
denatured calf-thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the catalytic specificity for ribonucleoside triphosphates vs. deoxynucleoside triphosphates during transcript elongation is 80
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
higher error ratios in transcription by RNA polymerase II are observed in the presence of Mn2+ compared to Mg2+. RNA polymerase II is able to elongate a primer with a 3'-terminal mismatch and thus to incorporate the mismatched nucleotide stable in the nascent RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
absolutely dependent on the presence of a double-stranded or single-stranded DNA template, with poly(dA-dT) DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Fremyella diplosiphon
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q83066
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme is highly active with poly dAT or T7 phage DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
mediates fast promoter-independent extension of unstable nucleic acid complexes, short DNA or RNA substrates are good substrates for the enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P00573
substrate specifically binds to the enzyme in the open conformation, where it is base paired with the acceptor template base, while Tyr639 provides discrimination of ribose versus deoxyribose substrates. Substrate selection occurs prior to the isomerization to the catalytically active conformation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme is able to use a variety of DNA templates. DNA from bacteriphage phiPLS27 is transcribed more efficiently than DNA isolated from lamda or herring sperm. DNA isolated from bacteriophage T7 and T7 D111 is utilized more efficiently
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
a kind of transcription complex is formed during RNA polymerase catalysed synthesis of the M13 bacteriophage replication primer. The complex contains an overextended RNA–DNA hybrid bound in the RNA-polymerase through that is normally occupied by downstream double-stranded DNA, thus leaving the 30 end of the RNA available for interaction with DNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Autographa californica M nucleopolyhedrovirus
-
Autographa californica M nucleopolyhedrovirus transcribes genes using two DNA-directed RNA polymerases. Early genes are transcribed by the host RNA polymerase II, and late and very late genes are transcribed by a viral-encoded multisubunit RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
enzyme is responsible for transcription in bacteria
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the hepatitis delta virus is an RNA virus that depends on DNA-dependent RNA polymerase for its transcription and replication. The association between human RNAP II and hepatitis delta virus RNA suggest two transcription start sites on both polarities of hepatitis delta virus RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the single subunit DNA-dependent RNA polymerase from bacteriophage T7 catalyzes both promoterdependent transcription initiation and promoter-independent elongation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, Q2XSM7
DNA-directed RNA polymerase activity
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
mechanism for de novo RNA synthesis, transcription begins with a marked preference for GTP at the +1 and +2 positions
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
T7 RNAP undergoes a slow conformational change to form an elongation competent complex with the promoter-free substrate. The complex binds to a correct NTP and incorporates the nucleoside monophosphate into RNA primer very efficiently. In the presence of inorganic pyrophosphate, the elongation complex catalyzes the reverse pyrophosphorolysis reaction at a maximum rate of 0.8 per s
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
two proton transfer occurs in the transition state for nucleotidyl-transfer reaction. Associative-like transition-state structure
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
recruitment of the enzyme is a rate-limiting step for the activation of the sigma(54) promoter Pu of Pseudomonas putida, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
minimal M13 origin hairpin is bound in the RNAP core channel normally occupied by dsDNA downstream of the transcription initiation start site, the sigma subunit is not required for initiation of RNA synthesis but it is essential for escape into productive elongation, RNAP recognition of the M13 ori and mechanism of RNA synthesis during transcription, detailed overview. During transcription elongation, RNAP can processively synthesize RNAs for thousands of nt. Mechanism of priming on dsDNA, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
regulation by anions, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression, synthesis of RNA transcripts of many thousands of nucleotides without dissociation. Energy, in the form of nucleoside triphosphates, fuels the synthesis of an RNA polymer complementary to specific regions of the DNA template. Like all macromolecular synthesis, RNA synthesis can be divided into three general phases: initiation, elongation, and termination. Importantly, each of these phases can be a target of regulation. Promoter recognition, binding at the extended promoter recognition region, and transcript initiation, RNAP prefers to initiate transcription within a narrow window located between 6 and 9 bp downstream of the -10 element, promoter clearance and elongation, termination and recycling, mechanisms and regulation , overview. The process of start site selection can be governed by the availability of either the +1 or the +2 NTP, depending on the promoter
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
RNAPIIis recruited to gene promoters in a hypo-phosphorylated state
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
transcription elongation as a critical regulatory step in addition to initiation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
DNA supercoiling-dependent and LSP-dependent RNA synthesis, three templates are used for in vitro RNA synthesis: the run-off template contains the light strand promoter, conserved sequence blocks, and heavy-strand origin. Promoter-independent RNA synthesis is dependent on DNA supercoiling and on TFB2M
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
in vitro transcription reactions with ATP, CTP, 3'-methyl-GTP, UTP, and DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
in vitro transcription reactions with ATP, CTP, GTP, UTP, and oligo(dC)-tailed DNA template derived from pAd-GR220
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
in vitro transcription with calf thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
supercoiled, double-stranded DNA template is more efficient than that from nonsupercoiled DNA, in vitro transcription activity and mechanism, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA, native or denatured, method evaluation: specificity and extent of transcription depends strongly on the quality of the DNA preparation, the strength of the promoter and terminator sequences, and the kind and concentration of mono- and divalent cations in the reaction mixture
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA, RNA translation process and mechanism of DNA-damage recognition by Pol II, detailed overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is plasmid DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is supercoiled DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
DNA-template dependent reaction. The best of the templates is phiH DNA, whereas T7 and T4 DNA are comparatively inactive and P2 DNA is a very weak template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
DNA-template dependent reaction. The enzyme transcribes phiH DNA as efficiently and T4 DNA as weakly as the Sulfolobus enzyme but T7 DNA even better than phiH DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Leishmania major MHOM/IL/81/Friedlin
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Leishmania sp. UR6
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Mycobacterium smegmatis mc2155
-
in vitro transcription with calf thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
DNA-template dependent reaction. The best of the templates is phiH DNA, whereas T7 and T4 DNA are comparatively inactive and P2 DNA is a very weak template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Thermoproteus tenax DSM 2078
-
DNA-template dependent reaction. The enzyme transcribes phiH DNA as efficiently and T4 DNA as weakly as the Sulfolobus enzyme but T7 DNA even better than phiH DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Pseudomonas putida PpY101
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme requires DNA as template, nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+
show the reaction diagram
Desulfurococcus mucosus, Desulfurococcus mucosus 07
-
DNA-template dependent reaction. T7 DNA and the plasmid PBR322 are by far the best templates. P2, T4 and T5 DNA are weak templates
-
-
?
nucleoside triphosphate + T10G2T2C2C
?
show the reaction diagram
-
oligonucleotide extension
-
-
?
rNTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q2WC24
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
dinucleoside teraphosphates are more potent substrates than dinucleoside triphosphates and dinucleoside pentaphosphates
-
-
-
additional information
?
-
-
determination of the substrate binding site
-
-
-
additional information
?
-
-
bacterial anti-sigma factors typically regulate sigma factor function by restricting the access of their cognate sigma-factors to the RNA polymerase RNAP core enzyme, regulation of RNAP holoenzyme, Esigma70, involving Rsd and the Rsd orthologue AlgQ, a global regulator of gene expression in Pseudomonas aeruginosa, which simultaneously interact with conserved region 2 and region 4 of sigma70 mediated by separate surfaces of Rsd, interaction with mutants of Rsd and AlgQ, mechanism, detailed overview. Rsd can strongly regulate the production of the Pseudomonas aeruginosa virulence factor pyocyanin in a manner that depends on their abilities to interact with sigma70 region 2
-
-
-
additional information
?
-
-
molecular mechanisms enabling sigma factor PvdS, directing the transcription of pyoverdine and virulence genes under iron limitation, to compete with the major sigma RpoD for RNA polymerase binding, overview
-
-
-
additional information
?
-
-
RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
-
-
-
additional information
?
-
-
intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions, overview
-
-
-
additional information
?
-
-
molecular mechanisms of transcription regulation in mitochondria, molecular organization of the human mitochondrial transcription initiation complex, overview
-
-
-
additional information
?
-
-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
-
-
-
additional information
?
-
-
multisubunit RNA polymerase transcribes DNA, but is also known to synthesize DNA replication primers in the replication system, a function that is commonly performed by primases, mechanism of primer synthesis by RNA polymerase and comparison to the mechanism of both types of primases, overview
-
-
-
additional information
?
-
P04050
peptide regions that interact with regulatory factors are close to the Pol II surface and assume seemingly flexible loop structures, one is located in the TFIIF-interacting protrusion domain, the other is located in the TFIIE-interacting clamp domain, conformations, overview
-
-
-
additional information
?
-
-
RNA pol III transcribes structural RNAs involved in RNA processing, U6 snRNA, and translation, tRNA. Mechanism of regulation of RNA pol III transcription by BRCA1, overview
-
-
-
additional information
?
-
-
RNA polymerase II phosphorylation during paused, active and poised transcription cycles with in itiation and elongation stages and at different phosphorylation stages, RNA polymerase II and histone modification profiles across genes in paused, active and poised states, and RNAPII regulation mechanisms at active genes, detailed overview. In embryonic stem cells, silent developmental regulator genes that are repressed by Polycomb are associated with a form of RNAPII that can elongate through coding regions but that lacks the post-translational modifications that are important for cou­pling RNA synthesis to co-transcriptional maturation
-
-
-
additional information
?
-
-
RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
-
-
-
additional information
?
-
-
RNAPII recruits COMPASS, a histone methyltransferase, as well as the regulator Paf1C, to the transcription active site causing methylation of histone H3K4 in a transcription-dependent manner. The large RNAPII subunit Rpb1 attracts FACT, a transcription factor that FACT participates in regulation of DNA repair and replication, to the transcription site, and Rpb1 also interacts with RSC, an abundant Swi/Snf-like chromatin remodeling complex with multiple subunits, and other general transcription factors, as well as with histone chaperone proteins, mRNA processing and export factors, DNA repair factors, protein kinases, and other cellular proteins, overview
-
-
-
additional information
?
-
-
the phosphatase activity of Cdc14 is required for Pol I inhibition, transcription inhibition is necessary for complete chromosome disjunction, because rRNA transcripts block condensin binding to rDNA, and show that bypassing the role of Cdc14 in nucleolar segregation requires in vivo degradation of nascent transcripts, transcription interferes with chromosome condensation, not the reverse
-
-
-
additional information
?
-
-
the PSi-C-terminal domain of large subunit RPB1 is essential for cell survivial and production of both SL RNA and mRNA, the Trypanosoma brucei enzyme lacks conserved heptapeptide sequence motifs found in most other eukaryotes
-
-
-
additional information
?
-
-
the Switch 1 loop of RNA polymerase II, located at the downstream end of the transcription bubble, may operate as a specific sensor of the nucleoside triphosphates available for transcription. Regulatory effects of RNA polymerase II on URA2 gene, encoding the rate-limiting enzyme of UTP biosynthesis after activation by UTP shortage, RNA polymerase II occupancy is increased on the URA2 open reading frame, overview
-
-
-
additional information
?
-
-
the two rpoB paralogues, rpoB(S) and rpoB(R), are two functionally distinct and developmentally regulated RNA polymerases, overview. A five amino acid substitutions located within or close to the so-called rifampin resistance clusters of rpoB(R) plays a key role in fundamental activities of the RNA polymerase. The rpoB(R)-specific missense mutation H426N is essential for the activation of secondary metabolism, molecular mechanism, overview
-
-
-
additional information
?
-
-
TLS regulates both RNAPs II and III and supports the possibility that cross-regulation between RNA polymerases is important in maintaining normal cell growth
-
-
-
additional information
?
-
-
two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
-
-
-
additional information
?
-
-
active site structure formed by amino acids from two domains: Palm with Asp457 and Asp695, and Fingers with Tyr537 and Lys529, overview
-
-
-
additional information
?
-
-
identification of an activity associated with the mtRNAP in which non-DNA-templated nucleotides are added to the 3' end of RNAs, any of the four rNTPs can act as precursors for this process, RNA editing mechanism, overview. Nucleotides that are not specified by the mitochondrial DNA templates are inserted into some RNAs, a process called RNA editing. This is an essential step in the expression of these RNAs, as the insertion of the nontemplated nucleotides creates open reading frames for the production of proteins from mRNAs or produces required secondary structure in rRNAs and tRNAs
-
-
-
additional information
?
-
O08348, P0A0Y1, Q8PC55, Q8PC56
in vitro transcriptional activity of recombinant assembled Xcc RNAP, overview
-
-
-
additional information
?
-
-
negative DNA supercoiling favors the induction of unpaired regions at some sequence motifs on dsDNA, substrate specificity and structural effects on activity, overview
-
-
-
additional information
?
-
-
RNAP adds nucleotides to the 3'-end of the growing RNA and translocates reiteratively, in single nucleotide steps. Translocation mechanism models, concerning conformational changes, allosteric effects and isomerization, and model evaluation, overview
-
-
-
additional information
?
-
-
the core enzyme, which lacks the sigma subunit, synthesizes short transcripts relatively uniformly on the DNA template in the presence of high concentrations of random primers and low NTP concentrations
-
-
-
additional information
?
-
-
the enzyme active site is located on the back wall of the channel, where an essential Mg2+ ion is chelated by three Asp of the absolutely conserved NADFDGD motif in the A' subunit
-
-
-
additional information
?
-
-
the enzyme also shows RNA-dependent RNA polymerase activity, EC 2.7.7.48, but slower and less processive than the DNA-dependent activity. During active transcription, Pol II must overcome intrinsic DNA-arrest sites, which are generally rich in A-T base pairs and pose a natural obstacle to transcription. At such sites, Pol II moves backwards along DNA and RNA, resulting in extrusion of the RNA 3' end through the polymerase pore beneath the active site and transcriptional arrest. The RNA cleavage stimulatory factor TFIIS can rescue an arrested polymerase by creating a new RNA 3' end at the active site from which transcription can resume, mechanism, overview
-
-
-
additional information
?
-
-
the RNAP clamp head domain constitutes the wall of the main channel opposite the catalytic centre and forms crucial contacts with the DNA template strand in the elongation complex
-
-
-
additional information
?
-
-
the RNAP purified from exponential phase shows low promoter specificity in promoter-polymerase interaction studies due to the presence of a large number of sigma factors during exponential phase and under-representation of sigma A required for house-keeping transcription
-
-
-
additional information
?
-
-
RNA polymerase III transcribes small untranslated RNAs that include tRNAs, 5S RNA, U6 RNA, and some microRNAs
-
-
-
additional information
?
-
-
the B2 family of short interspersed elements is transcribed into non-coding RNA by RNA polymerase III
-
-
-
additional information
?
-
-
dsDNA templates used for activity are T7A1_763, T7A1_437, T7A1_149, pcDNA3.1, pGEM, T-phage DNA, Escherichia coli DNA, calf thymus DNA, poly(dA-dT), and Kool NC-45
-
-
-
additional information
?
-
-
POLRMT can act as a primase in vitro and support lagging-strand DNA synthesis on a small 70 bp minicircle, overview
-
-
-
additional information
?
-
Leishmania major MHOM/IL/81/Friedlin
-
RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
-
-
-
additional information
?
-
Mycobacterium smegmatis mc2155
-
the RNAP purified from exponential phase shows low promoter specificity in promoter-polymerase interaction studies due to the presence of a large number of sigma factors during exponential phase and under-representation of sigma A required for house-keeping transcription
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q2XSM7
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q980R2, -
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the enzyme can bind to DNA containing the lambdaPR promoter, form an open complex and initiate transcription in a temperature-dependent manner. The organism relies on the high temperature of its environment to provide the thermal energy required to stimulate open promoter complex formation, initiate transcription, and facilitate the conformational changes in RNA polymerase that results in nucleotide incorporation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
mediates fast promoter-independent extension of unstable nucleic acid complexes
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
a kind of transcription complex is formed during RNA polymerase catalysed synthesis of the M13 bacteriophage replication primer. The complex contains an overextended RNA–DNA hybrid bound in the RNA-polymerase through that is normally occupied by downstream double-stranded DNA, thus leaving the 30 end of the RNA available for interaction with DNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Autographa californica M nucleopolyhedrovirus
-
Autographa californica M nucleopolyhedrovirus transcribes genes using two DNA-directed RNA polymerases. Early genes are transcribed by the host RNA polymerase II, and late and very late genes are transcribed by a viral-encoded multisubunit RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
enzyme is responsible for transcription in bacteria
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the hepatitis delta virus is an RNA virus that depends on DNA-dependent RNA polymerase for its transcription and replication. The association between human RNAP II and hepatitis delta virus RNA suggest two transcription start sites on both polarities of hepatitis delta virus RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
the single subunit DNA-dependent RNA polymerase from bacteriophage T7 catalyzes both promoterdependent transcription initiation and promoter-independent elongation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
recruitment of the enzyme is a rate-limiting step for the activation of the sigma(54) promoter Pu of Pseudomonas putida, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
minimal M13 origin hairpin is bound in the RNAP core channel normally occupied by dsDNA downstream of the transcription initiation start site, the sigma subunit is not required for initiation of RNA synthesis but it is essential for escape into productive elongation, RNAP recognition of the M13 ori and mechanism of RNA synthesis during transcription, detailed overview. During transcription elongation, RNAP can processively synthesize RNAs for thousands of nt. Mechanism of priming on dsDNA, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
regulation by anions, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression, synthesis of RNA transcripts of many thousands of nucleotides without dissociation. Energy, in the form of nucleoside triphosphates, fuels the synthesis of an RNA polymer complementary to specific regions of the DNA template. Like all macromolecular synthesis, RNA synthesis can be divided into three general phases: initiation, elongation, and termination. Importantly, each of these phases can be a target of regulation. Promoter recognition, binding at the extended promoter recognition region, and transcript initiation, RNAP prefers to initiate transcription within a narrow window located between 6 and 9 bp downstream of the -10 element, promoter clearance and elongation, termination and recycling, mechanisms and regulation , overview. The process of start site selection can be governed by the availability of either the +1 or the +2 NTP, depending on the promoter
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
RNAPIIis recruited to gene promoters in a hypo-phosphorylated state
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
transcription elongation as a critical regulatory step in addition to initiation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
-
-
?
GTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
bacterial anti-sigma factors typically regulate sigma factor function by restricting the access of their cognate sigma-factors to the RNA polymerase RNAP core enzyme, regulation of RNAP holoenzyme, Esigma70, involving Rsd and the Rsd orthologue AlgQ, a global regulator of gene expression in Pseudomonas aeruginosa, which simultaneously interact with conserved region 2 and region 4 of sigma70 mediated by separate surfaces of Rsd, interaction with mutants of Rsd and AlgQ, mechanism, detailed overview. Rsd can strongly regulate the production of the Pseudomonas aeruginosa virulence factor pyocyanin in a manner that depends on their abilities to interact with sigma70 region 2
-
-
-
additional information
?
-
-
molecular mechanisms enabling sigma factor PvdS, directing the transcription of pyoverdine and virulence genes under iron limitation, to compete with the major sigma RpoD for RNA polymerase binding, overview
-
-
-
additional information
?
-
-
RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
-
-
-
additional information
?
-
-
intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions, overview
-
-
-
additional information
?
-
-
molecular mechanisms of transcription regulation in mitochondria, molecular organization of the human mitochondrial transcription initiation complex, overview
-
-
-
additional information
?
-
-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
-
-
-
additional information
?
-
-
multisubunit RNA polymerase transcribes DNA, but is also known to synthesize DNA replication primers in the replication system, a function that is commonly performed by primases, mechanism of primer synthesis by RNA polymerase and comparison to the mechanism of both types of primases, overview
-
-
-
additional information
?
-
P04050
peptide regions that interact with regulatory factors are close to the Pol II surface and assume seemingly flexible loop structures, one is located in the TFIIF-interacting protrusion domain, the other is located in the TFIIE-interacting clamp domain, conformations, overview
-
-
-
additional information
?
-
-
RNA pol III transcribes structural RNAs involved in RNA processing, U6 snRNA, and translation, tRNA. Mechanism of regulation of RNA pol III transcription by BRCA1, overview
-
-
-
additional information
?
-
-
RNA polymerase II phosphorylation during paused, active and poised transcription cycles with in itiation and elongation stages and at different phosphorylation stages, RNA polymerase II and histone modification profiles across genes in paused, active and poised states, and RNAPII regulation mechanisms at active genes, detailed overview. In embryonic stem cells, silent developmental regulator genes that are repressed by Polycomb are associated with a form of RNAPII that can elongate through coding regions but that lacks the post-translational modifications that are important for cou­pling RNA synthesis to co-transcriptional maturation
-
-
-
additional information
?
-
-
RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
-
-
-
additional information
?
-
-
RNAPII recruits COMPASS, a histone methyltransferase, as well as the regulator Paf1C, to the transcription active site causing methylation of histone H3K4 in a transcription-dependent manner. The large RNAPII subunit Rpb1 attracts FACT, a transcription factor that FACT participates in regulation of DNA repair and replication, to the transcription site, and Rpb1 also interacts with RSC, an abundant Swi/Snf-like chromatin remodeling complex with multiple subunits, and other general transcription factors, as well as with histone chaperone proteins, mRNA processing and export factors, DNA repair factors, protein kinases, and other cellular proteins, overview
-
-
-
additional information
?
-
-
the phosphatase activity of Cdc14 is required for Pol I inhibition, transcription inhibition is necessary for complete chromosome disjunction, because rRNA transcripts block condensin binding to rDNA, and show that bypassing the role of Cdc14 in nucleolar segregation requires in vivo degradation of nascent transcripts, transcription interferes with chromosome condensation, not the reverse
-
-
-
additional information
?
-
-
the PSi-C-terminal domain of large subunit RPB1 is essential for cell survivial and production of both SL RNA and mRNA, the Trypanosoma brucei enzyme lacks conserved heptapeptide sequence motifs found in most other eukaryotes
-
-
-
additional information
?
-
-
the Switch 1 loop of RNA polymerase II, located at the downstream end of the transcription bubble, may operate as a specific sensor of the nucleoside triphosphates available for transcription. Regulatory effects of RNA polymerase II on URA2 gene, encoding the rate-limiting enzyme of UTP biosynthesis after activation by UTP shortage, RNA polymerase II occupancy is increased on the URA2 open reading frame, overview
-
-
-
additional information
?
-
-
the two rpoB paralogues, rpoB(S) and rpoB(R), are two functionally distinct and developmentally regulated RNA polymerases, overview. A five amino acid substitutions located within or close to the so-called rifampin resistance clusters of rpoB(R) plays a key role in fundamental activities of the RNA polymerase. The rpoB(R)-specific missense mutation H426N is essential for the activation of secondary metabolism, molecular mechanism, overview
-
-
-
additional information
?
-
-
TLS regulates both RNAPs II and III and supports the possibility that cross-regulation between RNA polymerases is important in maintaining normal cell growth
-
-
-
additional information
?
-
-
two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
-
-
-
additional information
?
-
-
RNA polymerase III transcribes small untranslated RNAs that include tRNAs, 5S RNA, U6 RNA, and some microRNAs
-
-
-
additional information
?
-
-
the B2 family of short interspersed elements is transcribed into non-coding RNA by RNA polymerase III
-
-
-
additional information
?
-
Leishmania major MHOM/IL/81/Friedlin
-
RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Fe-S cluster
-
with 4Fe-4S cluster-binding motif
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
can replace Mg2+ in activation, 10% of the activity observed with Mg2+
Iron
Q980R2, -
the enzyme possesses a unique Fe-S cluster
Iron
-
RNA polymerase is a member of the iron-sulfur cluster protein family and contains two 4Fe-4S cluster binding motifs
Iron
-
RNA polymerase is a member of the iron-sulfur cluster protein family
Iron
-
RNA polymerase is a member of the iron-sulfur cluster protein family and contains one 4Fe-4S cluster binding motif
K+
-
activates
K+
-
optimal activity at 0.02 M MgCl2 and 0.1 M KCl
KCl
-
maximal activity at 200 mM
KCl
-
optimal activity at pH 8.5 is obtained in presence of 18 mM MgCl2, 200 mM KCl, 1 mM thermine and 1 mM spermidine
KCl
-
maximal activity at 2 mM KCl
Mg2+
-
only limited ability to replace Mn2+
Mg2+
-
required, maximal activity at 10-20 mM
Mg2+
Fremyella diplosiphon
-
30 mM Mg2+ or 5 mM Mn2+ work equally well for maximal activity
Mg2+
-
required, maximal activity at 10-20 mM
Mg2+
-
maximal activity at 10-30 mM
Mg2+
-
highest activity is obtained with 20 mM Mg2+ on poly(dA-dT) DNA or Clostridium acetobutylicum DNA as template, with calf thymus DNA as template maximal activity is achieved with 10 mM Mg2+
Mg2+
-
higher error ratios in transcription by RNA polymerase II are observed in the presence of Mn2+ compared to Mg2+
Mg2+
-
optimal activity at pH 8.5 is obtained in presence of 18 mM MgCl2, 200 mM KCl, 1 mM thermine and 1 mM spermidine
Mg2+
-
maximal activity in presence of 5-10 mM MgCl2
Mg2+
-
required. Optimal activity at 10 mM MgCl2 and 50 mM NaCl
Mg2+
-
maximal activity at 15 mM MgCl2 or MnCl2
Mg2+
-
the active center of the enzyme involves a symmetrical pair of Mg2+ ions that switch roles in synthesis and degradation. One ion is retained permanently and the other is recruited ad hoc for each act of catalysis. The weakly bound Mg2+ is stabilized in the active center in different modes depending on the type of reaction: during synthesis by the beta,gamma-phosphates of the incoming substrate and during hydrolysis by the phosphates of a non-base-paired nucleoside triphosphate
Mg2+
-
required, optimal activity at 10 mM MgCl2
Mg2+
-
the enzyme active site is located on the back wall of the channel, where an essential Mg2+ ion is chelated by three Asp of the absolutely conserved NADFDGD motif in the A' subunit
Mg2+
-
-
Mg2+
-
bound at the active site
Mg2+
O08348, P0A0Y1, Q8PC55, Q8PC56
;
Mg2+
Q2WC24
essentially required, best at 10 mM
Mg2+
-
two ions are required for polymerase-catalyzed nucleotide incorporation, binding structure, overview
Mg2+
-
optimal activity at 0.02 M MgCl2 and 0.1 M KCl
Mn2+
-
2-4 mM required for optimal activity
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
Fremyella diplosiphon
-
30 mM Mg2+ or 5 mM Mn2+ work equally well for maximal activity
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
3 mM Mn2+ results in comparable activity with poly(dA-dT) DNA but reduced activity on calf thymus DNA or Clostridium acetobutylicum DNA and Clostridium acetobutylicum DNA as substrated, compared to Mg2+ activition
Mn2+
-
higher error ratios in transcription by RNA polymerase II are observed in the presence of Mn2+ compared to Mg2+
Mn2+
-
maximal activity at 15 mM MgCl2 or MnCl2
NaCl
-
optimal activity at 50 mM NaCl2
Zinc
-
a conserved zinc binding domain in the largest subunit of DNA-dependent RNA polymerase modulates intrinsic transcription termination and antitermination but does not stabilize the elongation complex
Mn2+
-
can partially replace Mg2+, 20% of the activity with Mg2+
additional information
-
KCl, ZnCl2 and CaCl2 can not replace MgCl2 in the assay mixture
additional information
-
the Pyrococcus RNA polymerase does not contain iron-sulfur cluster binding motifs
additional information
-
the Thermococcus RNA polymerase does not contain iron-sulfur cluster binding motifs
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
-
(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-3-(4-amino phenoxy)-5-methoxy phenyl acetate
-
-
(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-3-(4-aminophenoxy)-5-methoxyphenyl acetate
-
-
(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
1,3-dimethoxy-5-(4-nitrophenoxy) benzene
-
-
1-(3-C-ethynyl-beta-D-ribo-pentofuranosyl)cytosine
-
i.e. ECyd, TAS-106, a antitumor ribonucleoside that inhibits RNA polymerase, acts synergistically in inhibiting A-549 cancer cell growth and in tumor growth in vivo. The compound also inhibits the checkpoint-associated protein, the expression of Chk1 protein and the phosphorylation of Chk1 and Chk2, antitumour effects in combination with cisplatin, overview
1-[2-[3-(4-Chloro-3-trifluoromethylphenyl)ureido]-4-trifluoromethyl phenoxy]-4,5-dichlorobenzene sulfonic acid
-
-
2,4-dimethoxy-6-(4-nitrophenoxy) benzaldehyde
-
-
2-([[(1S)-2-amino-1-(4-hydroxybenzyl)-2-oxoethyl]amino]methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-acetyl-3-hydroxy-5-methoxyphenyl acetate
-
-
2-acetyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-formyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-hydroxy-4-methoxy-6-(4-nitrophenoxy) benzaldehyde
-
-
3'-ethynylcytidine-5'-triphosphate
-
i.e. ECTP, competitive inhibition in the presence of isolated nuclei from FM3A mouse tumor cells
4-[2-([[(1S)-2-amino-1-(4-hydroxybenzyl)ethyl]amino]methyl)-5-methoxy-3-(2-oxopropyl)benzyl]benzaldehyde
-
-
actinomycin
-
-
alpha-amanithin
-
-
alpha-amanithin
-
-
alpha-Amanitin
-
alpha-amanitin inhibits Pol II by trapping the wedged trigger loop and shifted bridge helix, thereby stabilizing a conformation of the elongation complex that apparently represents a translocation intermediate
alpha-Amanitin
-
the potent Sc RNAP II inhibitor binds to a ternary elongation complex with an open wedged conformation of the trigger loop
aureolic acid
-
-
B2 RNA
-
the about 180-nt B2 RNA potently represses mRNA transcription by binding tightly to RNA polymerase II and assembling with it into complexes on promoter DNA, where it keeps the polymerase from properly engaging the promoter DNA. The C-terminal domain of the largest Pol II subunit is not involved. B2 RNA binds Pol II and assembles into complexes at promoters. Binding site anaylsis usig Pol II peptides, binding structure, and mechanism of transcriptional repression by B2 RNA, detailed overview
-
breast cancer susceptibility gene 1
-
BRCA1, inhibits RNA pol III via inhibition of the essential transcription factor TFIIIB, mechanism, overview. BRCA1 is a tumor suppressor playing a role in DNA repair, cell cycle regulation, apoptosis, genome integrity, and ubiquitination, and it BRCA1 has a conserved N-terminal RING domain, an activation domain 1, AD1, and an acidic C-terminal domain, BRCA1 C-terminal region. Interaction with TFIIIB occurs via the BRCA1 C-terminal region domain of Fcp1p, an RNA polymerase II phosphatase. RNA pol III inhibition involves the TFIIB family members Brf1 and Brf2, overview
-
CBR703
-
the IC50s values are significantly decreased with template Kool NC-45, or increased with template poly(dA-dT)
Cdc14
-
a protein phosphatase required for nucleolar segregation and mitotic exit4, inhibits RNA polymerase I, the phosphatase activity of Cdc14 is required for Pol I inhibition in vitro and in vivo involving nucleolar exclusion of Pol I subunits
-
chromomycin
-
-
-
Cinerubin B
-
-
cisplatin
-
a single cisplatin 1,2-d(CG) intrastrand cross-link or a single cisplatin 1,3-d(GTG) intrastrand cross-link is a strong block to the enzyme. The efficiency of the block at a cisplatin 1,2-d(GG) intrastrand cross-link is similar in several different nucleotide sequence contexts. Some blockage is also observed when the single cisplatin 1,3-d(GTG) intrastrand cross-link is located in the non-transcribed strand. Cisplatin-induced lesions in the transcribed DNA strand constitute a strong physical barrier to RNA polymerase progression
corallopyronin
-
inhibition is not affected by template Kool NC-45
-
corallopyronin A
-
-
Cordycepin triphosphate
-
-
d(Ap4C)
-
d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
-
d(Ap4G)
-
d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
-
d(Ap4T)
-
d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
-
d(Tp4C)
-
d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
-
d(Tp4T)
-
d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
-
Echinomycin
-
-
Eruticulomycin A
-
-
-
Ethidium bromide
-
-
etnangien
-
from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien
-
from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin, poor inhibition
etnangien
-
from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien
-
from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, poor inhibition of the yeast enzyme
etnangien
-
from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien methyl ester
-
-
etnangien methyl ester
-
weak inhibition
etnangien methyl ester
-
very weak inhibition
etnangien methyl ester
-
-
etoposide
-
treatment with 0.02 mM etoposide leads to a transient inhibition of rRNA synthesis
Exotoxin of Bacillus thuringiensis
-
-
-
Isoquinocyclin
-
-
-
myxopyronin
-
produced by the bacteria Myxococcus fulvus, inhibits initiation of RNA polymerase transcription and binding complex structure. The compounds inhibits the enzyme also from rifamycin- or multidrug-resistant bacteria. the inhibition mechanism proceeds via inhibiting DNA binding rather than affecting transcription complex stability or processivity following DNA binding, overview
myxopyronin
-
inhibits bacterial RNA polymerase and inhibits transcription on the artificially melted promoters, inhibition mechanism, overview. The antibiotic binds to a pocket deep inside the RNAP clamp head domain, which interacts with the DNA template in the transcription bubble, binding of dMyx stabilizes refolding of the beta'-subunit switch-2 segment, resulting in a configuration that might indirectly compromise binding to, or directly clash with, the melted template DNA strand, binding structure, overview. Antibiotic binding does not prevent nucleation of the promoter DNA melting but instead blocks its propagation towards the active site. dMyx binds in the pocket deep inside the RNAP clamp head domain. Mutations designed in switch-2 mimic the dMyx effects on promoter complexes in the absence of antibiotic
myxopyronin
-
an alpha-pyrone antibiotic, targets the RNAP switch region, which is the hinge that mediates opening and closing of the RNAP active-center cleft. Lower values for inhibition by myxopyronin in the presence of template Kool NC-45
myxopyronin A
-
-
Nogalamycin
-
-
oxygen
-
the enzyme is highly oxygen sensitive. Inactivation is accompanied by cross-linking of components. Inactivated enzyme can be reactivated by reduction with sodium dithionite
procyclin-associated genes
-
i.e. PAG1, PAG2 or PAG3, inhibit RNA synthesis, deletion of PAGs lead to increased mRNA levels, regulation of PAG expressions, overview
-
proflavin sulfate
-
-
protein TLS
-
translocated in liposarcoma, a protein originally identified as the product of a chromosomal translocation, which associates with both RNAP II and the spliceosome, also represses transcription by RNAP III. It represses transcription from all three classes of RNAP III promoters in vitro and to associates with RNAP III genes in vivo. Depletion of TLS by siRNA in HeLa cells resulted in increased steady-state levels of RNAP III transcripts as well as increased RNAP III and TBP occupancy at RNAP III-transcribed genes
-
RBL-1
-
oligonucleotide, efficiently inhibits
-
RECQL5
-
a DNA helicase of the RECQ family, directly inhibits RNA polymerase II. It RECQL5 inhibits both initiation and elongation in transcription assays reconstituted with highly purified general transcription factors and RNAPII, RECQL5 helicase activity is not required for inhibition
-
Rifampicin
-
0.1 mg/ml, complete inhibition
Rifampicin
-
0.00006 mg/ml, 50% inactivation
ripostatin A
-
-
sorangicin A
-
-
Spt5
-
the large subunit of the DRB sensitivity-inducing factor, DSIF, represses or activates RNAPII elongation in vitro. CTR1 and CTR2CT, the two repeat-containing regions constituting the C-terminus of Spt5, play a redundant role in repressing RNAPII elongation in vivo, overview. Mutant NSpt5, lacking the C-terminus, directly associates with hsp70-4 chromatin in vivo and increases the occupancy of RNAPII, positive transcription elongation factor b, histone H3 Lys 4 trimethylation, and surprisingly, the negative elongation factor A at the locus, indicating a direct action of NSpt5 on the elongation repressed locus, nuclear extracts containing the constitutively active P-TEFb and WT DSIF lead to a time-dependent increase of the long, promoter-distal RNase T1-resistant products, reflecting the elongation stimulatory activity of Spt5, overview
-
Streptolydigin
-
the antibiotic binds to a Tt RNAP TEC with an open trigger loop
streptovaracin
-
-
-
streptovaricin
-
-
Tagetitoxin
-
inhibition of RNA polymerase III
Tagetitoxin
-
no inhibition of calf thymus RNA polymerase II
Tagetitoxin
-
inhibition of RNA polymerase III
Tagetitoxin
-
50% inhibition at 0.0001 mM. Complete inhibition at 0.01 mM
TFAM
-
DNA packaging by TFAM makes the DNA more resistant to unwinding
-
ureidothiophene
-
-
MnCl2
-
in presence of 10 mM MgCl2
additional information
-
no inhibition by NEM and iodoacetamide
-
additional information
-
no inhibition by epigallocatechin gallate
-
additional information
-
no inhibition by ent-16-ketobeyeran-19-oic acid, i.e. isosteviol, and related compounds
-
additional information
-
despite relatively high overall sequence and structural homology between bacterial and mammalian core RNAP enzymes, there are sufficient differences between the enzyme classes for exploitation in the discovery of selective bacterial inhibitors
-
additional information
-
gamma irradiation leads to a transient inhibition of rRNA synthesis, but Pol I transcription is not blocked by DNA damage itself, but by the action of DNA repair enzymes
-
additional information
-
inactivation of RNase P, by knockdown of RNase P subunits Rpp21, Rpp29 or Rpp38 by RNA interference, reduces the level of nascent transcription by Pol I, and more considerably that of Pol III, e.g. causing marked reduction in transcription of rDNA by Pol I
-
additional information
-
oncogenes and tumor suppressors control Pol I transcription, overview. Development of drugs that target the Pol I transcription machinery at different points, overveiw
-
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
no inhibition of RNA transcription by RECQL5 helicase-deficient point mutant RECQL5D157A, and another human RECQ family helicase, RECQL1
-
additional information
-
Top1 inhibition favors Pol II escape from a promoter-proximal pausing site of the human HIF-1alpha gene in living cells. Top1 inhibition can trigger a transcriptional stress, involving antisense transcription and increased chromatin accessibility, which is dependent on cdk activity and deregulated Pol II pausing
-
additional information
-
structure-based design of inhibitors with rifampicin as template, inhibitory potencies and binding mechanism via specific hydrogen-bonding sites involving residues Q390, F394, R405, Q567 and Q633, overview
-
additional information
-
a relatively short DNA region, lost in up2DELTA mutant and located immediately upstream of the URA2 initiator, impairs URA2 transcription by preventing RNA polymerase II from progressing towards the URA2open reading frame
-
additional information
-
the use of dsDNA templates containing classical promoters has only a negligible effects on the potency of enzyme inhibitors
-
additional information
-
POLRMT is an off target for antiviral ribonucleoside analogues, unique mechanisms of mitochondrial transcription inhibition, overview
-
additional information
-
FLiZ antagonize sigmaS-dependent gene expression in Escherichia coli. FliZ is an abundant DNA-binding protein and a global regulatory protein under the control of the flagellar master regulator FlhDC. It inhibits gene expression mediated by sigmaS by recognizing operator sequences that resemble the -10 region of sigmaS-dependent promoter. FLiZ plays a pivotal role in the decision between alternative life-styles, i.e. FlhDC-controlled flagellum-based motility or pS-dependent curli fimbriae-mediated adhesion and biofilm formation. FliZ is a global repressor with a DNA sequence specificity overlapping that of sigmaS–containing RNA polymerase, mechanism, overview
-
additional information
-
no inhibition by 0.1 mg/ml of rifampicin, streptolydigin or alpha-amanitin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CK2
-
is associated with Pol I, the initiation-competent subclass of Pol I, CK2 phosphorylates a number of proteins involved in Pol I transcription and pre-rRNA processing, including UBF, TIF-IA, SL1/TIF-IB, topoisomerase IIa, nucleolin, and nucleophosmin, overview
-
Ctk1
-
the kinase is required for the stability of the scaffold, but Ctk1 kinase activity is not required for the dissociation of basal transcription factors
-
PAF53
-
a 53-kDa protein that is associated with Pol I, recruitment of Pol I to the pre-initiation complex requires the interaction of UBF with SL1/TIF-IB and with PAF53
-
potassium acetate
-
activates
potassium aspartate
-
activates
potassium chloride
-
activates
potassium glutamate
-
activates highly, role of potassium ion in the activation of osmotic transcription
potassium nitrate
-
activates
Rho
-
in response to the Rho termination factor, RNA synthesis ceases and the completed transcript is released
-
RNase P
-
required for Pol I and Pol III required
-
sigma
-
a dissociable specificity sigma factor, regulated by factors such as anti-sigma factors, which can sequester r factors and prevent core association, and possibly by factors that enhance sigma-core association
-
sigma factor
-
a dissociable specificity sigma factor, regulated by factors such as anti-sigma factors, which can sequester sigma factors and prevent core association, and possibly by factors that enhance sigma-core association
-
sigma factor
-
required for activity
-
sigma70
-
the sigma factor increases the transcription efficiency of templates with nonphysiological nonprokaryotic promoters
-
spermidine
-
optimal activity at pH 8.5 is obtained in presence of 18 mM MgCl2, 200 mM KCl, 1 mM thermine and 1 mM spermidine
Spt5
-
the large subunit of the DRB sensitivity-inducing factor, DSIF, represses or activates RNAPII elongation in vitro. CTR1 and CTR2CT, the two repeat-containing regions constituting the C-terminus of Spt5, play a redundant role in repressing RNAPII elongation in vivo, overview. Mutant NSpt5, lacking the C-terminus, directly associates with hsp70-4 chromatin in vivo and increases the occupancy of RNAPII, positive transcription elongation factor b, histone H3 Lys 4 trimethylation, and surprisingly, the negative elongation factor A at the locus, indicating a direct action of NSpt5 on the elongation repressed locus, nuclear extracts containing the constitutively active P-TEFb and WT DSIF lead to a time-dependent increase of the long, promoter-distal RNase T1-resistant products, reflecting the elongation stimulatory activity of Spt5, overview
-
Spt6
-
transcription factor, Pol II shows a broad requirement for essential Spt6 during different stages of development, e.g. for for maximal recruitment of Paf1 and Spt5 to transcriptionally active Hsp70. Spt6 interacts with both nucleosome structure and Pol II, it has a role in elongation, directed RNAi knock-down of Spt6 reduces the elongation rate, the Spt6-dependent effect on elongation rate persists during steady-state-induced transcription, reducing the elongation rate from about 1100 to 500 bp/min. Stimulation of Pol II elongation rate by Spt6 is not mediated through transcription factor TFIIS
-
TAFI protein
-
performs important tasks in transcription complex assembly, mediating specific interactions between the rDNA promoter and Pol I, thereby recruiting Pol I, together with a collection of Pol I-associated factors, to rDNA
-
TFB2
-
the essential initiation factor forms a network of interactions with DNA near the transcription start site and facilitates promoter melting but may not be essential for promoter recognition, TFB2 bridges upstream and downstream promoter contacts of the initiation complex, mapping of TFB2-DNA interactions at the transcription start site, overview
-
TFB2M
-
the requirement for TFB2M in transcription of dsDNA is that it can stabilize an incompletely single-stranded template established by negative supercoiling
-
TFIIIE
-
a basal transcription factor, complexes with several ribosomal proteins and enhances tRNA and 5S rRNA transcription of the RNA polymerase, regualtion, overview
-
TFIIS
-
an RNA cleavage stimulatory factor TFIIS. TFIIS can rescue an arrested polymerase by creating a new RNA 3' end at the active site from which transcription can resume, mechanism, overview
-
Thermine
-
optimal activity at pH 8.5 is obtained in presence of 18 mM MgCl2, 200 mM KCl, 1 mM thermine and 1 mM spermidine
TIF-IB/SL 1
-
Pol I promoter specificity is conferred by TIF-IB/SL1, a protein complex containing the TATA binding protein and five TATA binding protein-associated factors, including TAFI110/95, TAFI68, TAFI48, TAFI35, and TAFI12
-
transcription factor TFIIIB
-
proper initiation by RNA pol III requires the transcription factor TFIIIB. Gene-external U6 snRNA transcription requires TFIIIB consisting of Bdp1, TBP, and Brf2. Transcription from the gene internal tRNA promoter requires TFIIIB composed of Bdp1, TBP, and Brf1. Breast cancer susceptibility gene 1, BRCA1, inhibits TFIIB, which interacts with the BRCA1 C-terminal region domain of Fcp1p, an RNA polymerase II phosphatase, TFIIIB regulation network, overview
-
upstream binding factor
-
UBF, activates rRNA gene transcription by several means, for example, by recruiting Pol I to the rDNA promoter, by stabilizing binding of TIF-IB/SL1, and by displacing nonspecific DNA binding proteins such as histone H1. And UBF has additional roles in regulation of Pol I promoter escape and transcription elongation
-
glutamate
-
glutamate remodels the sigma38 transcription complex for activation. Accumulation of the simple signaling molecule glutamate can reprogram RNA polymerase in vitro without the need for specific protein receptors. During osmotic activation, glutamate appears to act as a Hofmeister series osmolyte to facilitate promoter escape. Escape is accompanied by a remodeling of the key interaction between the sigma38 stress protein and the beta-flap of the bacterial core RNA polymerase. This activation event contrasts with the established mechanism of inhibition in which glutamate, by virtue of its electrostatic properties, helps to inhibit binding to ribosomal promoters after osmotic shock
additional information
-
Pol III initiates and reinitiates transcription in the absence or presence of transcription factors, during the first transcription cycle transcription factors IIIB and IIIC mainly contribute to the selectivity and not to the rate of Pol III association to the template, while their stable association with the promoter in subsequent cycles strongly contributes to the high rate of transcription reinitiation by Pol III
-
additional information
-
The activity of basal Pol I factors is regulated by posttranslational modifications
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
additional information
-
the Pol II transcription apparatus requires the transcription factors TBP, TFIIB, TFIIEalpha and TFIIS
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
additional information
-
the enzyme complex requires multiple transcription factors and protein interactions for activity, e.g. Spt6, overview
-
additional information
-
the enzyme complex requires basal transcription factors, i.e. TFIID, TFIIA, TFIIH, and TFIIE, for complete processing of transitions from initiation to elongation, overview
-
additional information
-
RNA polymerase complex with associated proteins, overview
-
additional information
-
mechanism of activation of antibiotic biosynthesis by Nonomuraea rpoB(R), overview
-
additional information
-
the RNA polymerase complex requires several transcription factors for activity, e.g. the general transcription factors, TBP, TFIIA, TFIIB, TFIIF, and TFIIE
-
additional information
-
interaction of elongation factors with RNAP, such as NusG and RfaH, affects the frequency and duration of pausing during transcription
-
additional information
-
intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions
-
additional information
-
RNAP contains the vegetative sigma subunit sigma70 (RpoD) and/or the flagellar sigma factor sigma28 (FliA)
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.018
-
A10G2A2C2C
-
-
-
0.041
-
A9G3A2C2C
-
-
-
0.0095
-
ATP
-
pH 7.9, 37°C, wild-type enzyme
0.016
-
ATP
-
pH 7.9, 37°C, mutant enzyme W422A
0.036
-
ATP
-
pH 7.9, 37°C, mutant enzyme Y427A
0.067
-
ATP
-
pH 7.9, 37°C, mutant enzyme D421A
0.137
-
ATP
-
pH 7.9, 37°C, mutant enzyme R423A
0.14
0.142
ATP
-
wild-type enzyme
0.282
-
ATP
-
pH 7.9, 37°C, mutant enzyme R425K
0.384
-
ATP
-
pH 7.9, 37°C, mutant enzyme R425A
0.143
0.18
CTP
-
wild-type enzyme
0.00211
-
d(Ap4T)
-
-
-
0.00222
-
d(Tp4C)
-
-
-
0.00174
-
d(Tp4G)
-
-
-
0.00072
-
d(Tp4T)
-
-
-
0.015
-
dGTP
-
pH 8.0, 37°C, dGTP as elongation substrate during dinucleotide synthesis, activation by Mg2+, mutant enzyme Y639F
0.025
-
dGTP
-
pH 8.0, 37°C, dGTP as elongation substrate during dinucleotide synthesis, activation by Mg2+, mutant enzyme Y639F
0.387
-
dGTP
-
pH 8.0, 37°C, dGTP as elongation substrate during dinucleotide synthesis, activation with Mn2+
0.75
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme Y639F
0.85
-
dGTP
-
pH 8.0, 37°C, dGTP as elongation substrate during dinucleotide synthesis, activation by Mg2+, wild-type enzyme
0.88
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, wild-type enzyme
1.1
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme Y639F/S641A
1.4
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, wild-type enzyme
0.0004
-
dTTP
-
-
1.2
-
dUTP
-
pH 8.0, 37°C, activation by Mg2+, wild-type enzyme
1.7
-
dUTP
-
pH 8.0, 37°C, activation by Mg2+, wild-type enzymes
0.043
-
G2CAC2C
-
-
-
0.1
-
GTP
-
pH 7.9, 23°C
1.6e-05
-
promoter complex
-
-
-
0.0103
-
rGTP
-
pH 8.0, 37°C, rGTP as elongation substrate during dinucleotide synthesis, activation by Mn2+, wild-type enzyme
-
0.0104
-
rGTP
-
pH 8.0, 37°C, rGTP as elongation substrate during dinucleotide synthesis, activation by Mg2+, mutant enzyme Y639F
-
0.0153
-
rGTP
-
pH 8.0, 37°C, rGTP as elongation substrate during dinucleotide synthesis, activation by Mn2+, mutant enzyme Y639F
-
0.0175
-
rGTP
-
pH 8.0, 37°C, rGTP as elongation substrate during dinucleotide synthesis, activation by Mg2+, wild-type enzyme
-
0.21
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme S641A
-
0.22
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme Y639F/S641A
-
0.25
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, wild-type enzyme
-
0.32
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme Y639F
-
0.036
-
rUTP
-
pH 8.0, 37°C, activation by Mn2+, wild-type enzyme
-
0.041
-
rUTP
-
pH 8.0, 37°C, activation by Mg2+, wild-type enzyme
-
0.0018
-
T10G2T2C2C
-
-
-
0.079
0.107
UTP
-
wild-type enzyme
0.234
-
GTP
-
wild-type enzyme
additional information
-
additional information
-
-
-
additional information
-
additional information
-
relative KM-values for UTP derivatives
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.26
-
A10G2A2C2C
-
-
-
4
-
A9G3A2C2C
-
-
-
0.00065
-
ATP
-
pH 7.9, 37°C, mutant enzyme R425A
0.0013
-
ATP
-
pH 7.9, 37°C, mutant enzyme R423A
0.005
-
ATP
-
pH 7.9, 37°C, mutant enzyme D421A
0.0135
-
ATP
-
pH 7.9, 37°C, mutant enzyme R425K
0.253
-
ATP
-
pH 7.9, 37°C, mutant enzyme Y427A
0.35
-
ATP
-
pH 7.9, 37°C, mutant enzyme W422A
0.482
-
ATP
-
pH 7.9, 37°C, wild-type enzyme
0.1
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme Y639F/S641A
0.22
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, wild-type enzyme
0.32
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme S641A
0.34
-
dGTP
-
pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme Y639F
8.3
-
promoter complex
-
-
-
0.25
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme Y639F/S641A
-
0.26
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, wild-type enzyme
-
0.28
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme Y639F
-
0.38
-
rGTP
-
pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme S641A
-
0.23
-
T10G2T2C2C
-
-
-
0.03
-
G2CAC2C
-
-
-
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000343
-
-
-
0.006
-
-
-
0.0156
-
-
-
4600
-
Q2WC24
purified recombinant His6-tagged enzyme, pH 7.9, 37°C
additional information
-
-
-
additional information
-
-
-
additional information
-
-
assay for RNA polymerase activity that uses the dye RiboGreen to detect transcripts by fluorescence and is thus free of the expense, short shelf life, and high handling costs of radioisotopes. The method is relatively quick and can be performed entirely in microplate formate, allowing for the processing of dozens to hundreds of samples in parallel
additional information
-
-
15.4% activity in rpoS-lacZ2 translational fusion PMP77F4 (delta 50 bp), relative to pMP77FK; 15.5% activity in rpoS-lacZ2 translational fusion PMP77F6 (delta 150 bp), relative to pMP77FK; 23.3% activity in rpoS-lacZ2 translational fusion PMP77FdeltaEI (delta 31 bp) , relative to pMP77FK; 35.8% activity in rpoS-lacZ2 translational fusion PMP77F5 (delta 100 bp), relative to pMP77FK; 36.1% activity in rpoS-lacZ2 translational fusion PMP77F7 (delta 200 bp), relative to pMP77FK; 55.7% activity in rpoS-lacZ2 translational fusion PMP77FdeltaE47III (delta 32 bp), relative to pMP77FK; 77.7% activity in rpoS-lacZ2 translational fusion PMP77F3 (relative to pMP77FK); 78.2% activity in rpoS-lacZ2 translational fusion PMP77FINEI (insertion 78 bp), relative to pMP77FK
additional information
-
-
-
additional information
-
O08348, P0A0Y1, Q8PC55, Q8PC56
recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega; recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega; recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega; recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
7.9
-
-
-
7.9
-
-
assay at
7.9
-
-
assay at
7.9
-
-
assay at
7.9
-
-
assay at
7.9
-
O08348, P0A0Y1, Q8PC55, Q8PC56
assay at; assay at
8
-
-
assay at
8
-
-
assay at
8.5
-
-
Tris-HCl buffer
9
-
-
glycine-NaOH buffer
10
-
-
poly(dA-dT) DNA as a template
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8.7
-
pH 7.0: about 75% of maximal activity, pH 8.7: about 75% of maximal activity
7
9
-
pH 7.0: about 30% of maximal activity, pH 9.0: about 60% of maximal activity
7.5
9
Q2WC24
80% of maximall activity within this range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28
-
O08348, P0A0Y1, Q8PC55, Q8PC56
assay at; assay at
30
-
-
assay at
30
-
-
assay at
35
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
40
45
-
with poly(dA-dT) DNA or Clostridium acetobutylicum DNA as template
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
Q2WC24
activity range, profile, overview
30
50
-
30°C: about 50% of maximal activity, 50°C: about 20% of maximal activity
37
50
-
37°C: about 25% of maximal activity, 50°C: about 5% of maximal activity
37
50
-
37°C: about 50% of maximal activity, 50°C: about 80% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
stably transfected with plasmid RPB3-SPB
Manually annotated by BRENDA team
-
in embryonic stem cells, silent developmental regulator genes that are repressed by Polycomb are associated with a form of RNAPII that can elongate through coding regions but that lacks the post-translational modifications that are important for cou­pling RNA synthesis to co-transcriptional maturation
Manually annotated by BRENDA team
-
IMR90 fibroblasts
Manually annotated by BRENDA team
Leishmania major MHOM/IL/81/Friedlin, Leishmania sp. UR6
-
-
-
Manually annotated by BRENDA team
additional information
-
intracellular levels of RNAP, RpoD and PvdS in strains PAO1 and W1485, quantification of RpoD- and PvdS-dependent RNAP holoenzymes, overview
Manually annotated by BRENDA team
additional information
-
aside from growth-dependent regulation, Pol I transcription also oscillates during cell cycle progression. Transcription is maximal during S- and G2-phase, subsides during mitosis, and then slowly recovers during G1-phase
Manually annotated by BRENDA team
additional information
-
RNAPII complexes are also located at silent genes in promoter-proximal paused configurations that provide dynamic transcriptional regulation downstream from ini­tiation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
74% of the RNA polymerase activity is associated with the rickettsial cell membrane at a high salt concentration, 600 mM NaCl
Manually annotated by BRENDA team
B2RFX8
N-terminal transit peptide of SmRpoT confers enzyme targeting to mitochondria
Manually annotated by BRENDA team
-
the enzyme in nucleus encoded and then transported to the mitochondrion
Manually annotated by BRENDA team
-
RNase P and Pol I are located at the promoter and coding region of rDNA
Manually annotated by BRENDA team
-
interchromatin granule clusters are the storage sites for the components of RNA polymerase II holoenzyme and other factors of RNA pol II transcription, such as CBP/p300, TATA-binding protein, and basal transcription factors TFIID and TFIIH, in transcriptionally inert oocytes, overview
Manually annotated by BRENDA team
-
distribution of TFIIB, TFIIH and RNA polymerase II at the URA2 locus, RNA polymerase II occupancy is increased on the URA2 open reading frame, overview
Manually annotated by BRENDA team
-
isozyme Pol IIIalpha and Pol IIIbeta, primarily
Manually annotated by BRENDA team
Saccharomyces cerevisiae yBC-10
-
-
-
Manually annotated by BRENDA team
additional information
B2RFX8
no evidence that Selaginella may contain a nuclear-encoded phage-type chloroplast RNA polymerase
-
Manually annotated by BRENDA team
additional information
-
the enzyme is encoded in the nucleus
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Enterobacteria phage N4
Enterobacteria phage N4
Enterobacteria phage N4
Enterobacteria phage N4
Enterobacteria phage N4
Enterobacteria phage N4
Enterobacteria phage N4
Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1)
Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1)
Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1)
Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1)
Escherichia coli (strain K12 / DH10B)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain J99 / ATCC 700824)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Yersinia pseudotuberculosis serotype I (strain IP32953)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20470
-
P39466
subunit E, calculated from sequence
30000
-
Q980R2, -
free enzyme, gel filtration
40600
-
Q980R2, -
enzyme D/L subcomplex, gel filtration
469000
-
-
core protein of Pol II
480000
-
-
glycerol gradient centrifugation
480000
-
-
about
500000
-
-
RNAP I and RNAP II, gel filtration
512000
-
-
holoenzyme complex of Pol II
562000
-
-
non-denaturing gel filtration
583000
-
-
gel filtration
600000
700000
-
RNAP III, gel filtration
620000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE; x * 185000 + x * 125000 + x * 47000 + x * 30000 + x * 93000, SDS-PAGE
?
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
?
Fremyella diplosiphon
-
x * 161000 + x * 134000 + x * 72000 + x * 41000 + x * 91000, SDS-PAGE; x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
?
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE; x * 190000 + x * 145000 + x * 72000 + x * 38000, SDS-PAGE
?
-
x * 151000 + x * 147000 + x * 55000 + x * 42000, SDS-PAGE
?
-
betax,beta‘x,alpha,x,sigmax, x * 140000 + x * 170000 + x * 40000 + x * 92000, SDS-PAGE
?
-
x * 146000, beta and beta‘ comigrate, + x * 105000, main sigma factor, + x * 40000, alpha, SDS-PAGE
?
-
betax,beta‘x,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
?
-
betax,beta‘x,sigmax,alphax, x * 148000 + x * 142000 + x * 85000 + x * 34500, SDS-PAGE
?
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
?
-
beta‘,beta,sigma,alpha occur with a stoichiometric ratio of 1:1:1:2, x * 184000 + x * 141000 + x * 55000 + x * 45000, SDS-PAGE
?
-
beta‘x,beta,sigma,alpha, x * 160000 + x * 145000 + x * 85000 + x * 40000, SDS-PAGE
?
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
?
-
the most probably subunit structure for the enzyme is the following: 154000 + 104000 + 77000 + 64000 + 52000 + 48000 + 46000 + 45000 + 39000
?
-
beta‘x,betax,alphax,sigmax,sigma‘x, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
?
-
x * 25608, RpoE2, sequence calculation, x * 20103, RpoE3, sequence calculation
?
-
x * 99000, T7 polymerase-like structure
?
P11521
x * 100000, SDS-PAGE; x * 9460, calculated from sequence
?
Leishmania sp. UR6
-
the most probably subunit structure for the enzyme is the following: 154000 + 104000 + 77000 + 64000 + 52000 + 48000 + 46000 + 45000 + 39000
-
?
Pseudomonas putida PpY101
-
betax,beta‘x,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
-
?
-
x * 25608, RpoE2, sequence calculation, x * 20103, RpoE3, sequence calculation
-
?
-
x * 100000, SDS-PAGE; x * 9460, calculated from sequence
-
decamer
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
decamer
-
core protein of Pol II
dodecamer
-
holoenzyme complex of Pol II
dodecamer
-
the Rpb2 subunit of RNAP II combines with the Rpb1 subunit to form the RNAP II active site. RNAP II is isolated as a 12 subunit enzyme, Rpb1-Rpb12
dodecamer
Saccharomyces cerevisiae yBC-10
-
the Rpb2 subunit of RNAP II combines with the Rpb1 subunit to form the RNAP II active site. RNAP II is isolated as a 12 subunit enzyme, Rpb1-Rpb12
-
heterotrimer
-
the three subunits, PB1, PB2 and PA, are all required for both transcription and replication, PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA, whose C-terminal domain consists of 13 alpha-helices and 9 beta-strands, is involved in assembly of the functional complex. The subunit interface is important for virla replication, overview
monomer
-
-
monomer
Q2WC24
1 * 100000, SDS-PAGE
multimer
-
bacterial RNAP is a multisubunit enzyme and consists of a core polymerase containing the beta, beta' , and two alpha subunits, together with one or more omega subunits, and a dissociable specificity factor sigma
oligomer
-
beta',beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
oligomer
-
RNA polymerase III contains seventeen subunits. The Schizosaccharomyces pombe subunits are expressed in Saccharomyces cerevisiae null mutants and tested for growth. Ten core subunits show heterospecific complementation, but the two largest catalytic subunits (Rpc1 and Rpc2) and all five RNA polymerase III-specific subunits (Rpc82, Rpc53, Rpc37, Rpc34 and Rpc31) are non-functional. Three highly conserved RNA polymerase III-specific domains are found in the twelve-subunit core structure. They correspond to the Rpc17-Rpc25 dimer, involved in transcription initiation, to an N-terminal domain of the largest subunit Rpc1 important to anchor Rpc31, Rpc34 and Rpc82, and to a C-terminal domain of Rpc1 that presumably holds Rpc37, Rpc53 and their Rpc11 partner
oligomer
Autographa californica M nucleopolyhedrovirus
-
the viral RNA polymerase is composed of four proteins: Late Expression Factor-4 (LEF-4), LEF-8, LEF-9, and P47. Associations are observed between LEF-9 and P47, LEF-4 and P47, and LEF-8 and P47. LEF-4 and LEF-8 do not coimmunoprecipitate but coimmunoprecipitated in the presence of P47, suggesting that they do not associate directly. A weak association is observed between LEF-4 and LEF-9. LEF-8, LEF-9, and P47 have the ability to self-associate
oligomer
-
several subunits, e.g. subunit C of 44 kDa
oligomer
-
RNAPII structure and modeling of the multi-subunit enzyme complex, RNAP subunits can be divided into three groups concerned with catalysis, assembly of the catalytic subunits and auxiliary functions, overview
oligomer
-
structure and modeling of the multi-subunit enzyme complex, RNAP subunits can be divided into three groups concerned with catalysis, assembly of the catalytic subunits and auxiliary functions, overview. The large A and B subunits are split into two polypeptides, A'/A'' and B''/B' according to size, they harbour the binding sites for substrate NTPs, duplex DNA template and a 9 bp DNA-RNA hybrid, and provide the catalytic centre, including three catalytic aspartic acid residues and two Mg2+ ions
oligomer
-
alpha2betabeta'omega structure and modeling of the multi-subunit enzyme complex, RNAP subunits can be divided into three groups concerned with catalysis, assembly of the catalytic subunits and auxiliary functions, overview
pentamer
-
subunits structure alpha2betabeta'sigmaomega
monomer
-
the enzyme consists of three distinct regions, a catalytic C-terminal polymerase domain (residues 648-1230), an N-terminal domain (residues 369-647) and an N-terminal extension (residues 1-368), domain architecture, overview. The POLRMT C-terminal domain is characteristic of the Pol I family of nucleic acid polymerases, typically described as resembling the shape of a cupped right hand, containing the fingers, palm and thumb subdomains. The palm subdomain contains several key structural motifs that are highly conserved among the different classes of nucleic acid polymerases. The N-terminal extension contains the mitochondrial targeting sequence (residues 1-41), a large, flexible region of unknown structure (residues 42-217) and a pentatricopeptide repeat domain (residues 218-368). The pentatricopeptide repeat domain is connected to the N-terminal domain via a short proline-rich linker region that likely functions as a spacer connecting the two domains. The pentatricopeptide repeat domain consists of two tandem PPR motifs, the domnain contains nine alpha-helices of which four comprise the pentatricopeptide repeat motifs
additional information
-
multi-subunit enzyme
additional information
-
dimer-monomer formation is reversible and the equilibrium depends on the ionic strength of the medium. At high ionic strength the enzyme dissociates to a monomeric form
additional information
Q83066
the gene locus for the largest subunit is identified and its primary structure is determined
additional information
-
existence of two possible conformers: E and E‘ that are in rapid equilibrium. Both forms can form the quarternary complex, but only the E form is capable of catalyzing phosphodiester bond formation
additional information
-
binding of the sigma70 subunit to the core enzyme induces conformational changes in a single-stranded DNA binding region of the protein. As a consequence of these conformational changes, sigma70 subunit gains the specificity for the nontemplate strand of the melted region in the open complex
additional information
-
the core of the procaryotic RNAP comprises five subunits
additional information
-
subunits RPB5 and RPB6 localize to discrete subnuclear compartments and form part of different polymerase complexes. RNA interference mediated depletion of these discrete subunits abolishes class-specific transcription
additional information
-
at 0.5 M NH4CI the enzyme exists in the monomeric form
additional information
-
peptide and subunit mapping for determination of the substrate binding site
additional information
-
subunit RpoS of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genesin gram-negative bacteria.
additional information
-
the bacterial RNAP uses a homodimeric assembly platform
additional information
-
analysis of interaction sbetween the largest subunit Rpb1 and the other subunits, overview
additional information
-
conformational plasticity of the active center and importance of the bridge helix structure for enzyme activity, overview
additional information
-
the enzyme lacks the Rpb8 and Rpo13 subunits
additional information
-
structure analysis and modeling, overview
additional information
-
structure analysis, overview, the enzyme contains a subunit Rpo13 located at a groove between the H subunit and the clamp head domain of the A' subunit, model ing including the A' subunit jaw and clamp head domains and RpoG and Rpo13, overview
additional information
P04050
peptide regions that interact with regulatory factors are close to the Pol II surface and assume seemingly flexible loop structures, one is located in the TFIIF-interacting protrusion domain, the other is located in the TFIIE-interacting clamp domain, conformations, e.g. of the TFIIF-interacting Rpb2 protrusion, overview. Conformational movement and dynamics of fork loop-1 and -2. mechanism, overview
additional information
-
the PSi-C-terminal domain of large subunit RPB1 is essential for cell survivial and production of both SL RNA and mRNA, the Trypanosoma brucei enzyme lacks conserved heptapeptide sequence motifs found in most other eukaryotes
additional information
P36594
enzyme structure analysis and comparison to the structures of Saccharomyces cerevisiae and human Pol IIs, overview
additional information
-
detailed RNAPII structure study in different comformations, e.g. concerning the trigger loop, using crystal structures, the collective set of all normal modes describes enzyme flexibility as a function of residue in terms of root mean square fluctuations, RMSF values are directly related to crystallographic B-factors, enzyme motions described by individual modes, caclulations, overview
additional information
-
3D structure of the RNA polymerase from the mitochondrial plasmid is T7 polymerase-like, modeling using molecular mechanics and molecular dynamics, overview
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea. The enzyme lacks the G and M polypeptides
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea. The enzyme lacks the G subunit
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea. The enzyme lacks the G subunit
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
the enzyme consists of three distinct regions, a catalytic C-terminal polymerase domain, an N-terminal domain and an N-terminal extension, a pentatricopeptide repeat domain is not present in the yeast enzyme
additional information
-
RNAP contains the vegetative sigma subunit sigma70 (RpoD) and/or the flagellar sigma factor sigma28 (FliA)
additional information
-
components of the RNA polymerase and their molecular weights determined by SDS-PAGE
additional information
Desulfurococcus mucosus 07
-
components of the RNA polymerase and their molecular weights determined by SDS-PAGE
-
additional information
Pseudomonas putida WCS358
-
subunit RpoS of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genesin gram-negative bacteria.
-
additional information
Sulfolobus acidocaldarius DSM 639, Thermoproteus tenax DSM 2078
-
components of the RNA polymerase and their molecular weights determined by SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
RNAPIIis recruited to gene promoters in a hypophosphorylated state, but is phosphorylated at Ser5, Ser7, and Ser2. Its escape from the promoter requires TFIIH-mediated phosphorylation of Ser5, the onset of productive elongation requires P-TEFb, which phosphorylates Ser2 residues of the RNAPII C-terminal domain to produce stable elongation com­plexes. Absence of Ser 2Pat poised RNAPIIcomplexes is likely to disrupt co-transcriptional RNAmaturation and histone modification to help maintain the silent state, whereas binding and transcription by RNAPII counteract Polycomb-mediated chromatin conden­sation
phosphoprotein
-
RNA Pol II phosphorylation at Ser5 within the C-terminal domain
phosphoprotein
-
RNA Pol II phosphorylation at Ser5 within the C-terminal domain
ubiquitination
-
nondegradative ubiquitylation of RNA Pol II subunit Rpb1
phosphoprotein
-
the yeast Ctk1 kinase associates with elongation complexes and phosphorylates serine 2 in the YSPTSPS repeats of the RNApII large subunit Rpb1 C-terminal domain, a modification that is necessary for efficient recruitment of the Set2 methyltransferase to RNApII within transcribed regions and for coupling transcription to mRNA 3'-end processing, but Ser2 phosphorylation of the Rpb1 CTD does not regulate the 5' transitions. Ctk1 kinase activity is not required for the dissociation of basal transcription factors
side-chain modification
-
mapping of methylation and acetylation sites, all observed N-methylated lysines are on the surface of the enzyme
side-chain modification
-
mapping of methylation and acetylation sites, all observed methyl-lysines are on the surface of the enzyme
phosphoprotein
-
phosphorylation of polymerase large subunit RPB1
additional information
-
The activity of basal Pol I factors is regulated by posttranslational modifications, overview, e.g. acetylation is a posttranslational modification that regulates the activity of basal Pol I transcription factors, including UBF and SL1/TIF-IB
additional information
-
in embryonic stem cells, silent developmental regulator genes that are repressed by Polycomb are associated with a form of RNAPII that can elongate through coding regions but that lacks the post-translational modifications that are important for cou­pling RNA synthesis to co-transcriptional maturation
phosphoprotein
-
RNAPII C-terminal heptarepeat domain is subject to phosphorylation, e.g. at Ser5 and Ser7, during initiation and elongation of transcription by RNA polymerase II, e.g. by cyclin-dependent kinase 7, CDK7. Phosphorylation of both Ser5 and Ser7 is fully dependent on the cofactor complex Mediator. A subform of Mediator associated with an active RNAPII is critical for preinitiation complex formation and CTD phosphorylation. Free RNAPII that is recruited to templates in the absence of Mediator is not efficiently phosphorylated by CDK7. The Mediator-RNAPII complex independently recruits TFIIB and CDK7 to core promoter regions. CDK7 phosphorylates Ser7 selectively in the context of an intact preinitiation complex, inhibition by roscovitine, molecular mechanisms, overview
additional information
-
The activity of basal Pol I factors is regulated by posttranslational modifications, overview, e.g. acetylation is a posttranslational modification that regulates the activity of basal Pol I transcription factors, including UBF and SL1/TIF-IB
additional information
-
several posttranslational modifications of the large subunit of RNA polymerase II, Rpb1, including hydroxylation of Pro1465, nondegradative ubiquitylation of RNA Pol II, and phosphorylation of Ser5. Induction of Rpb1 hydroxylation, phosphorylation, and ubiquitylation requires the presence of the von Hippel-Lindau protein, overview
ubiquitination
-
nondegradative ubiquitylation of RNA Pol II subunit Rpb1
additional information
-
several posttranslational modifications of the large subunit of RNA polymerase II, Rpb1, including hydroxylation of Pro1465, nondegradative ubiquitylation of RNA Pol II, and phosphorylation of Ser5. Induction of Rpb1 hydroxylation, phosphorylation, and ubiquitylation requires the presence of the von Hippel-Lindau protein, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure determination
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
-
crystallographic structure at 4.0 A
-
T7 RNAP elonation complex
-
crystal structure anaysis
-
a large fragment of subunit PA bound to a fragment of subunit PB1, hanging dropn vapour diffusion method, 20°C, mixing of 0.001 ml of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM sodium chloride, and 0.001 ml of reservoir solution consisting of 100mM Tris-HCl, pH 7.5, and 2.4 M sodium formate, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
-
crystal structure determination
-
ammonium sulfate precipitation
-
crystal structure of the core enzyme at about 3.3 A resolution
-
crystallization of RNA polymerase II elongation complex. The purified paused complex forms crystals capable of X-ray diffraction to 3,5 A resolution. The complex remains active in the crystal and, in the presence of nucleoside triphosphates, can efficiently extend the transcript in situ
-
crystals are grown by the sitting drop vapor diffusion method, crystal structure of RNA polymerase II in the act of transcription is determined at 3.3 A resolution
-
glycerol precipitation, two-dimensional crystals of RNA polymerase I dimers are obtained upon interaction with positively charged lipid layers
-
hanging-drop vapour diffusion method. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
-
in complex with alpha-amanitin, hanging drop vapour diffusion method, with 200 mM ammonium acetate, 300 mM sodium acetate, 50 mM HEPES, pH 7.0, 4-7% (w/v) PEG 6000 and 5 mM Tris(2-carboxyethyl) phosphine
-
in order to obtain an atomic model of the complete Pol II, atomic models of the core Pol II at 2.8 A resolution and of the additional heterodimeric subcomplex of subunits Rpb4 and Rpb7 at 2.3 A resolution are combined and refined against the diffraction data obtained from a holo-Pol II crystal at 3.8 A resolution, method optimization
-
purified Pol II, X-ray diffraction structuredetermination and analysis at 3.8 A resolution, single anomalous diffraction from zinc ions bound intrinsically in Pol II
P04050
two-dimensional crystals are obtained by interaction with positively charged lipid layers. The enzyme is preferentially oriented by the lipid phase
-
Pol II in complex with transcription factor TFIIB, sessile drop-vapor diffusion method, 11 mg/ml protein in 10 mM Tris-HCl, pH 7.5, 25 mM KCl, 0.1 mM EDTA, 0.001 mM ZnCl2, 10 mM DTT, and 14.2 mM pentaethyleneglycol monooctyl ether, is mixed with an equal volume of reservoir solution containing 50 mM MES, pH 6.3, 300 mM ammonium acetate, 5-6.5% w/v PEG 4000, and 10 mM DTT, 9 days at 16°C, crystals are crushed and microseeded into a fresh drop prepared as before except with MES, pH 6.6, and 3.6% PEG 4000. After several rounds of microseeding, long rod-shaped crystals are obtained, cryoprotection by 15-30% glycerol, X-ray difraction structure determination and analysis at 3.65 A resolution. molecular modelling
P36594
crystal structure determination
-
crystallization of the enzyme with DNA fragments, crystal growth is optimized using a nanoseeding technique, of the various crystals screened, one diffracts to 4.3 A resolution
-
microbatch under oil technique, hanging-drop vapour diffusion technique, crystal structure at 3.35 A resolution
-
vapour diffusion technique using nanolitre sitting-drop, crystal structures of the DNA-bound and free form of the enzyme
B8YB53
crystal structure determination, structure including the A' subunit jaw and clamp head domains and RpoG and Rpo13 subunits
-
crystal structure of the core enzyme at about 3.3 A resolution
-
free enzyme and D/L subcomplex of archaeal RNAP, X-ray diffraction structure determination and analysis at 3.4 and 1.7 A resolution, respectively
Q980R2, -
crystal structure of the core enzyme at 3.3 A resolution
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
Q2WC24
half-life time of K1E RNAP stored in buffer containing 20 mM Na3PO4, 100 mM NaCl, pH 7.7, 1 mM EDTA, 10 mM DTT, and 0.1% Triton X-100, supplemented with 50% glycerol, is 87 h
30
-
-
10 min, stable
40
-
-
10 min, slight inactivation
50
-
-
10 min, slight inactivation
50
-
Q2WC24
half-life time of the K1E RNAP is 16.5 sec
80
-
-
15 min, 2% loss of activity
95
-
-
15 min, 50% loss of activity
100
-
-
15 min, 65% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
40% glycerol is absolutely required for stability
-
enzyme shows an extreme instability in the presence of salts
Fremyella diplosiphon
-
each freeze-thaw cycle results in significant loss of activity
-
nucleolar enzyme appears to be less stable than the nucleoplasmic enzyme, particularly in the presence of salt
-
the two largest Pol I subunits do not dissociate from one another between rounds of transcription. Pol I is relatively stable through multiple rounds of transcription
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the enzyme is highly oxygen sensitive. Inactivation is accompanied by cross-linking of components. Inactivated enzyme can be reactivated by reduction with sodium dithionite
-
724896
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, 60 mM Tris-HCl buffer, pH 7.8, 20 mM NH4Cl, 1 mM EDTA, 10 mM 2-mercaptoethanol, 40% glycerol, stable for several months
-
4°C, -20°C or -70°C, 50% w/v glycerol, stable for more than 3 months
-
the purified enzyme activity is stable in solution at 4°C even at low ionic strength and in the absence of bivalent metal ions or glycerol, storage in a buffer of low ionic strength containing no bivalent metal ions but 0.001 M EDTA and 10% glycerol at -70°C
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
PCC 7120
-
recombinant C-terminally His9-tagged enzyme to 90% purity by nickel affinity chromatography
-
recombinant His6-tagged K1E from Escherichia coli strain BL21(DE3) by nickel affinity chromatgraphy, dialysis and ultrafiltration
Q2WC24
recombinant His-tagged subunits PA and PB1 from Escherichia coli by nickel affinity chromatography
-
IgG-Sepharose beads chromatography
-
RNAP rom Mycobacterium smegmatis from exponential phase
-
RNA polymerase/N-terminal maltose binding protein (MBP) fusion protein
-, Q2XSM7
RNAP purification from iron-starved Pseudomonas aeruginosa cells
-
chromatography
-
recombinant wild-type and mutant RNAP II proteins
-
RNA polymerase II
-
polyethylene imine precipitation, anion exchange chromatography, heparin and T4-DNA affinity chronatography, and sucrose gradient centrifugation
-
recombinant enzymes partially from Escherichia coli
Q980R2, -
recombinant Xcc core RNAP subunits from Escherichia coli by a two-step chromatographic process; recombinant Xcc core RNAP subunits from Escherichia coli by a two-step chromatographic process; recombinant Xcc core RNAP subunits from Escherichia coli by a two-step chromatographic process; recombinant Xcc core RNAP subunits from Escherichia coli by a two-step chromatographic process
O08348, P0A0Y1, Q8PC55, Q8PC56
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
genes for the subunits beta and beta‘
-
gene rpoA, recombinant expression of the C-terminally His9-tagged enzyme in Escherichia coli B834 (DE3) cells, subcloning in Escherichia coli strain DH5alpha
-
gene k1ep, expression of His6-tagged K1E in Escherichia coli strain bL21(DE3), recombinant expression of K1E RNA polymerase in Bacillus megaterium strain MS941, a nprM deletion mutant of DSM319, using K1E promoters or SP6 promoter and a PEG-mediated transformation, method development and evaluation. The T7 RNAP promoter is not recognized at all
Q2WC24
construction of plasmids with polylinker cloning sites adjacent to the RNA polymerase promoter
-
expression of the T7 RNA polymerase tagged with yellow fluorescent protein and His6 in Rhodobacter capsulatus strain B10S establishing an additional expression system for the enzyme, method optimization and system evaluation, comparison to the Escherichia coli strain BL21(DE3) expression system, both using the expression vector pRhotHi-2-yfp-His6, overview. T7 RNA polymerase subcloning in Escherichia coli strain DH5alpha. Quantitative expression analysis, overview
-
the genes rpoA, rpoB and rpoC which encode the RNA polymerase, alpha-, beta- and beta‘subunits, respectively, have been individually placed on expression plasmids under control of the bacteriophage T7 promoter. Induction of the T7 RNA polymerase gene in hist cells harbouring each of the three plasmids, results in the extensive overproduction of the three polypeptides
-
gene rpoA, library screening
-
isolation and characterisation of a cDNA encoding the RNA polymerase common subunit RPB6
-
expressed in HEK-293T cells, HAT-1080 cells, and Magi cells
-
expression of the N-terminally His6-tagged intein fusion mitoRNAP protein
-
stable ectopic expression of subunit RPC32alpha in IMR90 fibroblasts
-
expression of His-tagged subunits PA and PB1 in Escherichia coli
-
mitochondrial plasmid sequence determination and analysis, the viral-like RNA polymerase ORF has 3' and 5' inverted terminal repeats, also a 5' binding protein. This protein can be involved in both replication and integration processes of these plasmid in the mitochondrial genome
-
rpoB(R) markedly activates antibiotic biosynthesis in the wild-type Streptomyces lividans strain 1326 and also in strain KO-421, a relaxed mutant unable to produce ppGpp, phenotypes, overview
-
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
-
cloning of the cDNA for the mtRNAP of Physarum and expression in Escherichia coli
-
expressed in Escherichia coli as an N-terminal maltose binding protein (MBP) fusion protein
-, Q2XSM7
Production of different translational and transcriptional fusions in Escherichia coli. PCR fragments of different sizes are cloned into plasmids resulting in intermediate constructs.
-
overexpression of His6-tagged subunit D of the RNA polymerase. A shuttle expression vector system for Pyrococcus furiosus and Escherichia coli is described allowing the regulated expression of proteins in Pyrococcus. A shuttle vector of Pyrococcus abyssi is redesigned using the overexpression of the HMG-CoA reductase as a selection marker which confers resistance to the antibiotic simvastatin
-
recombinant Rpb2 R512C, TAP-tagged at the C-terminus of the RNAP II Rpb9 subunit
-
RPB2 gene encoding the Rpb2 subunit of yeast RNAP II, expression of mutant enzyme and subunits in Escherichia coli strain XL-1 Blue
-
expression in Saccharomyces cerevisiae
-
subunit 3 gene, rpb3
-
gene rpoT, single copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic structure and phylogenetic analysis, N-terminal transit peptide of SmRpoT confers targeting of green fluorescent-tagged protein exclusively to mitochondria after transient expression in Arabidopsis thaliana and Selaginella moellendorffii protoplasts
B2RFX8
genes rpoE2 and rpoE3, phage library screening, DNA and amino acid sequence determination and analysis, genetic organization and associated sigma factors, phylogenetic analysis of the sigma factors, overview
-
cloning of the genes for the three large subunits A, B and C, which are organized in line in the order B-A-C, genetic organization, DNA and amino acid sequence determination and anaylsis, the three RNA polymerase subunit genes are cotranscribed together with an ORF of 88 amino acid residues length situated immediately upstream of the B gene and two ORFs of 104 and 130 amino acid residues following the C gene, overview
-
expression in a phage display using Halobacterium phage phi H, method overview
-
genes encoding subunits of the enzyme, DNA and amino acid sequence determination and analysis, genetic organization involving the genes of the transcription machinery, i.e. gene tfis; genes encoding subunits of the enzyme, DNA and amino acid sequence determination and analysis, genetic organization involving the genes of the transcription machinery, i.e. gene tfis
P46217, Q07271
expression in Escherichia coli
Q980R2, -
identification and sequencing of the SK7 promoter, sequence comparison of the porcine SK7 snRNA with sequences from other organisms, overview
-
the genes for the large subunits beta and beta‘ are cloned and sequenced. MW for beta‘ and beta, calculated from nucleotide sequence is 190522 Da and 143139 Da
-
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
D2SMJ0
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
D2SMK0
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
-
expression of C-terminally His-tagged alpha subunit-encoded by gene rpoA, and coexpression of the subunits of Xanthomonas campestris pv. campestris core RNAP from plasmid pBBad22K in Escherichia coli strain BL21(DE3), overexpression with or without omega; expression of C-terminally His-tagged alpha subunit-encoded by gene rpoA, and coexpression of the subunits of Xanthomonas campestris pv. campestris core RNAP from plasmid pBBad22K in Escherichia coli strain BL21(DE3), overexpression with or without omega; expression of C-terminally His-tagged alpha subunit-encoded by gene rpoA, and coexpression of the subunits of Xanthomonas campestris pv. campestris core RNAP from plasmid pBBad22K in Escherichia coli strain BL21(DE3), overexpression with or without omega; expression of C-terminally His-tagged alpha subunit-encoded by gene rpoA, and coexpression of the subunits of Xanthomonas campestris pv. campestris core RNAP from plasmid pBBad22K in Escherichia coli strain BL21(DE3), overexpression with or without omega
O08348, P0A0Y1, Q8PC55, Q8PC56
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mitotic silencing of Pol I transcription is caused by Cdk1/cyclin B-dependent phosphorylation of a single threonine residue Thr852 at TAFI110 that impairs the interaction of SL1/TIF-IB with UBF
-
at the end of mitosis, Cdc14B, a phosphatase that is sequestered in an inactive state in the nucleolus during interphase and is released from rDNA during mitosis, dephosphorylates Thr852, thereby activating SL1 and relieving mitotic repression of Pol I transcription
-
mitotic silencing of Pol I transcription is caused by Cdk1/cyclin B-dependent phosphorylation of a single threonine residue Thr852 at TAFI110 that impairs the interaction of SL1/TIF-IB with UBF
-
at the end of mitosis, Cdc14B, a phosphatase that is sequestered in an inactive state in the nucleolus during interphase and is released from rDNA during mitosis, dephosphorylates Thr852, thereby activating SL1 and relieving mitotic repression of Pol I transcription
-
expression of rpoB(R) increases after transition to stationary phase due to five amino acid substitutions located within or close to the so-called rifampin resistance clusters that play a key role in fundamental activities of RNA polymerase
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D421A
-
mutation results in an enzyme with reduced activity and altered patterns of transcription
D421T
-
mutation results in an enzyme with reduced activity and altered patterns of transcription
R423A
-
mutation results in an enzyme with reduced activity and altered patterns of transcription
R423K
-
mutation results in an enzyme with reduced activity and altered patterns of transcription
R425K
-
mutation results in an enzyme with reduced activity and altered patterns of transcription
S641A
-
mutation reduces activity in presence of Mg2+ to 93% of the activity of the wild-type enzyme
W422A
-
mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme
W422F
-
mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme
W422R
-
mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme
W422S
-
mutation results in an enzyme that has nearly normal levels of activity and exhibitspatterns of transcription that arew similar to that of the wild-type enzyme
Y639/S641A
-
mutation reduces activity in presence of Mg2+ to 89% of the activity of the wild-type enzyme
Y639C
-
mutation reduces activity in presence of Mg2+ to 7.5% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 11
Y639F
-
mutation reduces the catalytic specificity for ribonucleoside triphosphates vs deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme by a factor of 20 and largely eliminates the KM-difference between rNTPs and dNTPs. The remaining specificity factor of 4 is turnover-number-mediated and is nearly eliminated if Mn2+ is substituted for Mg2+ in the reaction. Mn2+ substitution does not significantly affect the Km difference between rNTPs and dNTPs
Y639F
-
the fraction of catalytically active E form is 32% compared to 100% for the wild-type enzyme
Y639H
-
mutation reduces activity in presence of Mg2+ to 3.7% of the activity of the wild-type enzyme
Y639L
-
mutation reduces activity in presence of Mg2+ to 43% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 11
Y639M
-
mutation reduces activity in presence of Mg2+ to 50% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 5.5
Y639Q
-
mutation reduces activity in presence of Mg2+ to 1% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates vs deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 4.5
Y639T
-
mutation reduces activity in presence of Mg2+ to 1.3% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 6.5
Y639V
-
mutation reduces activity in presence of Mg2+ to 4.3% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 19
C70A/C72H/C85A/C88H
-
mutant enzyme is defective in intrinsic termination and antitermination in vitro. Mutation likely causes a recessive-lethal phenotype
C70H
-
mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
C72H
-
mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
C85H
-
mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
del70-88insGGGG
-
mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
del74-84insGGGG
-
mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
E813A/D814A
-
significantly decreased elongation rate, the mutation changes the effect of diphosphate on the 3'-5'-exonuclease reaction, whose addition stimulates the production of UMP through hydrolysis rather than of UTP through diphosphorolysis. The mutation makes the 3'-exonuclease activity independent of TTP. The mutation changes the response of TEC to diphosphate: instead of causing diphosphorolysis it stimulates the exonuclease reaction
N458A
-
significantly decreased elongation rate
R1106A
-
significantly decreased elongation rate, enhanced exonuclease activity
E244stop
-
random mutagenesis, identification of mutant L33, a truncated protein that lacks the C-terminal alpha-subunit, alphaCTD, but is capable of being assembled into the RNAP and carrying out transcription, while it does not respond to signals in the DNA or from protein effectors, overview. The mutant grows faster and exhibits a higher accumulated cell mass than the wild-type in the presence of butanol, phenotype, overview
V257F/L281P
-
random mutagenesis, the rpoA14 mutant shows mutations of the C-terminal alpha-subunit, phenotype, overview
V257R
-
random mutagenesis, the rpoA22 mutant shows a mutation of the C-terminal alpha-subunit, phenotype, overview
L640D
-
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
L666D
-
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
V636S
-
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
W706A
-
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
R584A
-
site-directed mutagenesis, the RNAP holoenzyme containing this sigma70 mutant binds preferentially to promoters bearing a specifically mutated -35 element
D505A
-
mutation in subunit Rpb2, the mutant shows a weak defect in the escape from a transcriptional stall at A20
E1028Q
-
mutation in subunit Rpb2, the mutant shows transcription elongation defects
E529A
-
mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
E529A
-
the substitution mutant is are faster than the wild-type enzyme in RNA elongation
E529D
-
mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
E529D
-
the substitution mutant is are faster than the wild-type enzyme in RNA elongation
E529Q
-
the substitution mutant is are slower than the wild-type enzyme in RNA elongation
G985A/G987A
-
the double substitution in subunit Rpb2 is expected to subtly affect the conformation and/or dynamics of K987, an essential residue
K979Q
-
lethal mutation in subunit Rpb2
K979R
-
lethal mutation in subunit Rpb2
K987Q
-
lethal mutation in subunit Rpb2
Q513A
-
mutation in subunit Rpb2, the mutant shows a weak defect in the escape from a transcriptional stall at A20
R1020K
-
lethal mutation in subunit Rpb2
R1020Q
-
lethal mutation in subunit Rpb2
R512A
-
mutation in subunit Rpb2, the mutant shows transcription elongation defects
R512C
-
mutation in subunit Rpb2, the mutant shows transcription elongation defects
R512C
-
site-directed mutagenesis, the highly conserved residue is located about 20 A from Mg2+-I and just C-terminal to the fork loop, molecular dynamics simulations, overview. Mutant Sc Rpb2 R512C is slow in elongation and shows transcriptional defects. Rpb2 R512C may have a defect in CTP-Mg2+ sequestration
R766A
-
the substitution is lethal, consistent with an important role for this invariant latch residue
R766Q
-
the substitution is lethal, consistent with an important role for this invariant latch residue
D505A
Saccharomyces cerevisiae yBC-10
-
mutation in subunit Rpb2, the mutant shows a weak defect in the escape from a transcriptional stall at A20
-
E529A
Saccharomyces cerevisiae yBC-10
-
mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
-
K631R
-
the fraction of catalytically active E form is 38% compared to 100% for the wild-type enzyme. The synthesis of long transcripts is markedly diminished for the mutant due to decreasing processivity
additional information
-
RNAP mutants: the N-terminal region of T7 RNAP contains a nascent RNA binding site that functions to retain the nascent chain within the ternary complex. The region surrounding residue 240 is involved in binding the initiating NTP. Residues at the very C terminus of T7 RNAP are involved in binding the elongating NTP
G711K/N926S/N1103S/N1117S
-
site-directed mutagenesis, the mutant mitoRNAP that lacks four natural hydroxylamine cleavage sites
additional information
-
combined shRNA and dsRNA POLRMT gene silencing
additional information
-
suppression of subunit RPC32alpha expression in HeLa cells by siRNAs. Levels of p53 and lamin A/C are dramatically downregulated by ectopic RPC32alpha expression, but either unchanged (lamin A/C) or moderately increased (p53) by ectopic RPC32beta subunit expression
H426N
-
the rpoB(R)-specific missense mutation is essential for the activation of secondary metabolism, molecular mechanism, overview
additional information
-
phenotypes of several sigma70 mutants and of diverse rsd mutants, genetic screening for isolating enhanced-function Rsd mutants, overview. Interaction of Rsd and AlgQ mutants with region 2 and 4 of sigma70, overview
K987R
-
lethal mutation in subunit Rpb2
additional information
-
mutations are made in highly conserved residues Rpb2 K979, K987, and R1020 within the active site region of RNAP II, at positions that potentially might be essential for catalytic function. Mutations are constructed in an extended fork region of subunit Rpb2, residues R504-E529, construction of diverse mutant strains, e.g. strain yBC-9 expressing subunit Rpb2 under the control of the Gal promoter and is deleted for the chromosomal copy of the DST1 gene, encoding transcription factor IIS, TFIIS. From the strain yBC-9, the strain yBC-32 was constructed by transformation with pFL39-RPB2-TAP, TRP1
additional information
-
mutagenesis by amino-acid replacements altering the RNA polymerase II Switch 1 loop domain, such as rpb1-L1397S. rpb1-L1397S enhances RNA polymerase II occupancy downstream of the URA2 initiator
E529D
Saccharomyces cerevisiae yBC-10
-
mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
-
additional information
Saccharomyces cerevisiae yBC-10
-
mutations are made in highly conserved residues Rpb2 K979, K987, and R1020 within the active site region of RNAP II, at positions that potentially might be essential for catalytic function. Mutations are constructed in an extended fork region of subunit Rpb2, residues R504-E529, construction of diverse mutant strains, e.g. strain yBC-9 expressing subunit Rpb2 under the control of the Gal promoter and is deleted for the chromosomal copy of the DST1 gene, encoding transcription factor IIS, TFIIS. From the strain yBC-9, the strain yBC-32 was constructed by transformation with pFL39-RPB2-TAP, TRP1
-
R512C
Saccharomyces cerevisiae yBC-10
-
mutation in subunit Rpb2, the mutant shows transcription elongation defects
-
additional information
-
the enzyme is chemically modified with AMP o-formylphenyl ester followed by reduction with borohydride, the modified protein catalyzes the labeling of its own largest subunit when incubated with [alpha33P]UTP in the presence of poly[d(A-T)], followed by mapping through using cyanogen bromide, hydroxylamine, or amino acid-specific endoproteinases, overview
additional information
-
simulation of diverse McJ25-resistant mutations and their effects on enzyme activity, overview
R428A
-
site-directed mutagenesis, designed based on substitutions at the homologous position (Rpb2 R512) of Saccharomyces cerevisiae RNAP II, used as a reference structure, molecular dynamics simulations with starting Tt RNAP TEC structure, PDB 205J, that is in a strained, catalytic conformation that responds very sensitively to the R428A substitution but is stable for wild-type enzyme, overview. Long range conformational coupling linking a dynamic segment of the bridge alpha-helix, the extended fork loop, the active site, and the trigger loop-trigger helix is apparent and adversely affected in beta R428A RNAP. The R428A substitution is instable in the i+1 dTMP-ATP base pair, as indicated by fluctuations in the dTMP O4-ATP N6 base pairing distance in R428A
additional information
-
RNAi-targeting of mRNA 39UTR allows regulated depletion of RPB1, mutant RNAP-II containing 1/3 Psi-C-terminal domain is defective in transcription and causes abortive initiation, it is toxic and causes cell death, while a 2/3 Psi-C-terminal domain mutant maintains steady-state transcript levels and still supports cell growth,, overview
additional information
O08348, P0A0Y1, Q8PC55, Q8PC56
recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP; recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP; recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP; recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
assembly of Xcc core RNAP subunits recombinantly coexpressed in Escherichia coli after purification by a two-step chromatographic process; assembly of Xcc core RNAP subunits recombinantly coexpressed in Escherichia coli after purification by a two-step chromatographic process; assembly of Xcc core RNAP subunits recombinantly coexpressed in Escherichia coli after purification by a two-step chromatographic process; assembly of Xcc core RNAP subunits recombinantly coexpressed in Escherichia coli after purification by a two-step chromatographic process including nickel affinity chromatography
O08348, P0A0Y1, Q8PC55, Q8PC56
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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the enzyme is useful for in vitro transcription reactions to produce preparative quantities of transcribed RNAand labeled RNA probes, transcripts thousands of nucleotides in length, as are the major applications of these reactions, method evaluation, overview. Phage SP6 RNA polymerase is an extremely processive enzyme in high-yield transcription of DNA sequences inserted downstream from the corresponding SP6 promoter, applications overview
synthesis
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the enzyme is useful for in vitro transcription reactions to produce preparative quantities of transcribed RNAand labeled RNA probes, transcripts thousands of nucleotides in length, as are the major applications of these reactions, method evaluation, overview. Phage T3 RNA polymerase is an extremely processive enzyme in high-yield transcription of DNA sequences inserted downstream from the corresponding T3 promoter, applications overview
synthesis
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the enzyme is useful for in vitro transcription reactions to produce preparative quantities of transcribed RNA and labeled RNA probes, transcripts thousands of nucleotides in length, as are the major applications of these reactions, method evaluation, overview. Phage T7 RNA polymerase is an extremely processive enzyme in high-yield transcription of DNA sequences inserted downstream from the corresponding T7 promoter, applications overview
analysis
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assay for RNA polymerase activity that uses the dye RiboGreen to detect transcripts by fluorescence and is thus free of the expense, short shelf life, and high handling costs of radioisotopes. The method is relatively quick and can be performed entirely in microplate formate, allowing for the processing of dozens to hundreds of samples in parallel
medicine
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the enzyme is a promising target for the discovery of new antimicrobial agents
synthesis
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the enzyme is useful for in vitro transcription reactions to produce preparative quantities of transcribed RNA and labeled RNA probes, method evaluation, overview
drug development
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development of drugs that target the Pol I transcription machinery at different points for use in cancer therapies, overview
drug development
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the enzyme is a target for drug design