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Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession P39466

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.6 DNA-directed RNA polymerase
IUBMB Comments
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).
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Sulfolobus acidocaldarius
UNIPROT: P39466
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Word Map
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase ii, pol ii, t7 rna polymerase, rna polymerase i, pol iii, rna polymerase iii, pol i, rnapii, rnap ii, dna-dependent rna polymerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DNA-dependent RNA polymerase
-
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
nucleotidyltransferase, ribonucleate
-
-
-
-
Pol II
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 polymerase
RNA polymerase I
-
-
-
-
RNA polymerase II
-
-
-
-
RNA polymerase III
-
-
-
-
RNA transcriptase
-
-
-
-
RNAP I
-
-
-
-
RNAP II
-
-
-
-
RNAP III
-
-
-
-
transcriptase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY hide
9014-24-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
additional information
?
-
-
determination of the substrate binding site
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
optimal activity at 0.02 M MgCl2 and 0.1 M KCl
Mg2+
-
optimal activity at 0.02 M MgCl2 and 0.1 M KCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no inhibition by 0.1 mg/ml of rifampicin, streptolydigin or alpha-amanitin
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit E
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20470
subunit E, calculated from sequence
100000
x * 100000, SDS-PAGE
101000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
10800
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
11200
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
11800
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
122000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
13800
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
17500
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
24000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
32000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
44000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
9460
x * 9460, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
oligomer
-
several subunits, e.g. subunit C of 44 kDa
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
mapping of methylation and acetylation sites, all observed N-methylated lysines are on the surface of the enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
LITERATURE
polyethylene imine precipitation, anion exchange chromatography, heparin and T4-DNA affinity chronatography, and sucrose gradient centrifugation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zillig, W.; Stetter, K.O.; Janekovic, D.
DNA-dependent RNA polymerase from the archaebacterium Sulfolobus acidocaldarius
Eur. J. Biochem.
96
597-604
1979
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Grachev, M.A.; Mustaev, A.A.; Zaychikov, E.F.; Lindner, A.J.; Hartmann, G.R.
Localisation of the binding site for the initiating substrate on the RNA polymerase from Sulfolobus acidocaldarius
FEBS Lett.
250
317-322
1989
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Phler, G.; Lottspeich, F.; Zillig, W.
Organization and nucleotide sequence of the genes encoding the large subunits A, B and C of the DNA-dependent RNA polymerase of the archaebacterium Sulfolobus acidocaldarius
Nucleic Acids Res.
17
4517-4534
1989
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Langer, D.; Zillig, W.
Putative tfIIs gene of Sulfolobus acidocaldarius encoding an archaeal transcription elongation factor is situated directly downstream of the gene for a small subunit of DNA-dependent RNA polymerase
Nucleic Acids Res.
21
2251
1993
Sulfolobus acidocaldarius (P46217), Sulfolobus acidocaldarius (Q07271), Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Kwapisz, M.; Beckouet, F.; Thuriaux, P.
Early evolution of eukaryotic DNA-dependent RNA polymerases
Trends Genet.
24
211-215
2008
Saccharomyces cerevisiae, Cenarchaeum symbiosum, Escherichia coli, Emiliania huxleyi, Methanocaldococcus jannaschii, Pyrococcus furiosus, Sulfolobus acidocaldarius, Saccharolobus solfataricus, Nanoarchaeum equitans, Caldivirga maquilingensis, Nitrosopumilus maritimus, Thermofilum pendens
Manually annotated by BRENDA team
Prangishvilli, D.; Zillig, W.; Gierl, A.; Biesert, L.; Holz, I.
DNA-dependent RNA polymerase of thermoacidophilic archaebacteria
Eur. J. Biochem.
122
471-477
1982
Desulfurococcus mucosus, Sulfolobus acidocaldarius, Thermoproteus tenax, Sulfolobus acidocaldarius DSM 639, Thermoproteus tenax DSM 2078, Desulfurococcus mucosus 07
Manually annotated by BRENDA team
Azkargorta, M.; Wojtas, M.; Nicola, A.; Elortza, F.
Lysine methylation mapping of crenarchaeal DNA-directed RNA polymerases by collision-induced and electron-transfer dissociation mass spectrometry
J. Proteome Res.
13
2637-2648
2014
Sulfolobus acidocaldarius, Saccharolobus shibatae
Manually annotated by BRENDA team
Langer, D.; Lottspeich, F.; Zillig, W.
A subunit of an archaeal DNA-dependent RNA polymerase contains the S1 motif
Nucleic Acids Res.
22
694
1994
Sulfolobus acidocaldarius (P39466)
Manually annotated by BRENDA team
Phler, G.; Leffers, H.; Gropp, F.; Palm, P.; Klenk, H.P.; Lottspeich, F.; Garrett, R.A.; Zillig, W.
Archaebacterial DNA-dependent RNA polymerases testify to the evolution of the eukaryotic nuclear genome
Proc. Natl. Acad. Sci. USA
86
4569-4573
1989
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
Manually annotated by BRENDA team
Klenk, H.P.; Palm, P.; Lottspeich, F.; Zillig, W.
Component H of the DNA-dependent RNA polymerases of Archaea is homologous to a subunit shared by the three eucaryal nuclear RNA polymerases
Proc. Natl. Acad. Sci. USA
89
407-410
1992
Sulfolobus acidocaldarius (P11521), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (P11521)
Manually annotated by BRENDA team