Information on EC 2.7.7.19 - polynucleotide adenylyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
2.7.7.19
-
RECOMMENDED NAME
GeneOntology No.
polynucleotide adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
also acts slowly with CTP, catalyses template-dependent extension of the 3'-end of a DNA strand by one nucleotide at a time, cannot initiate a chain de nove, the primer, depending on source of the enzyme, may be an RNA or DNA fragment, or oligo(a) bearing a 3'-OH terminal group, see also EC 2.7.7.6 DNA-directed RNA polymerase
-
-
-
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
mechanism
-
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
SN2-in-line-mechanism
-
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
binding of enzyme to nuclear poly(A) binding protein results in 80-fold increase in apparent affinity for RNA, mechanism
-
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
Arabidopsis possesses 4 genes for PAP, these genes are expressed at the level of mRNA in tissue-specific ways, transcripts from the four genes are alternatively spliced so as to yield mRNAs encoding highly truncated polypeptides; Arabidopsis possesses 4 genes for PAP, these genes are expressed at the level of mRNA in tissue-specific ways, transcripts from the four genes are alternatively spliced so as to yield mRNAs encoding highly truncated polypeptides; Arabidopsis possesses 4 genes for PAP, these genes are expressed at the level of mRNA in tissue-specific ways, transcripts from the four genes are alternatively spliced so as to yield mRNAs encoding highly truncated polypeptides; Arabidopsis possesses 4 genes for PAP, these genes are expressed at the level of mRNA in tissue-specific ways, transcripts from the four genes are alternatively spliced so as to yield mRNAs encoding highly truncated polypeptides
-, Q7XJ91, Q7XJ92, Q9LMT2
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
non-uniform isomerization of the polymerase-primer complex with time consistent with a discontinuous (saltatory) translocation mechanism. Three distinct translocatory phases can be discerned: a -10(U)-binding site forward movement, a -27/-26(UU)-binding site jump to -10, then a -27/-26(UU)-binding site movement further downstream. Poly(A) tail elongation shows no apparent pauses during these isomerizations
-
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
initial interaction between RNA and the enzyme is characterized by a high enthalpy of association. The minimal RNA binding site of the enzyme is eight nucleotides. Upon RNA binding, the enzyme undergoes structural modifications, although the interaction does not significantly modify the stability of the protein
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:polynucleotide adenylyltransferase
Also acts slowly with CTP. Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH terminal group. See also EC 2.7.7.6 DNA-directed RNA polymerase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenosine triphosphate:ribonucleic acid adenylyltransferase
-
-
-
-
AMP polynucleotidylexotransferase
-
-
-
-
ATP-polynucleotide adenylyltransferase
-
-
-
-
ATP:polynucleotidylexotransferase
-
-
-
-
Cid1
-
putative cytoplasmic PAP, in addition to having PAP activity, Cid1 possesses substantial poly(U) polymerase activity
Cid14
Schizosaccharomyces pombe ATCC 24843
Q9UTN3
-
-
germline development 2
Q6PIY7
-
GLD2
Q6PIY7
-
GLD4
Q6PIY7
-
Hs2
-
contains two PAP-associated domains and two nucleotidyl transferase motifs
neo-PAP
-
-
-
-
NTP polymerase
-
-
-
-
nuclear speckle targeted PIPKIalpha regulated-poly(A) polymerase
-
-
nucleotidyltransferase, polyadenylate
-
-
-
-
PAP
-
-
-
-
PAP
P25500
-
PAP
P0ABF1
-
PAP
Escherichia coli K12
P0ABF1
-
-
PAP
-
PAP is a template-independent polymerase that belongs to the DNA polymerase beta family of enzymes
PAP I
-
-
-
-
Pap II
-
-
PAPbeta
-
testis-specific PAP
PapD1
Q9NVV4
-
PapD5
Q8NDF8
-
PAPgamma
-
-
poly(A) hydrolase
-
-
-
-
poly(A) polymerase
-
-
-
-
poly(A) polymerase
-
-
poly(A) polymerase
O82312
PAP II
poly(A) polymerase
Q7XJ91
PAP IV
poly(A) polymerase
Q7XJ92
PAP III
poly(A) polymerase
Q9LMT2
PAP I
poly(A) polymerase
-
-
poly(A) polymerase
-
-
poly(A) polymerase
-
-
poly(A) polymerase
-
-
poly(A) polymerase
-
-
poly(A) polymerase
P0ABF1
-
poly(A) polymerase
Escherichia coli K12
P0ABF1
-
-
poly(A) polymerase
-
-
poly(A) polymerase
-
-
poly(A) polymerase
-
-
-
poly(A) polymerase
-
-
poly(A) polymerase
-
-
poly(A) polymerase gamma
-
-
poly(A) polymerase I
-
-
poly(A) polymerase II
-
-
poly(A) synthetase
-
-
-
-
poly(A)-polymerase
-
-
poly(A)polymerase I
-
-
polyA polymerase
-
-
polyadenylate nucleotidyltransferase
-
-
-
-
polyadenylate polymerase
-
-
-
-
polyadenylate polymerase
-
-
polyadenylate polymerase
-
-
polyadenylate synthetase
-
-
-
-
polyadenylic acid polymerase
-
-
-
-
polyadenylic polymerase
-
-
-
-
RNA adenylating enzyme
-
-
-
-
RNA formation factors, PF1
-
-
-
-
terminal riboadenylate transferase
-
-
-
-
Tpap
-
testis-specific PAP
Tpap
-
testis-specific poly(A) polymerase
ZCCHC6
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-30-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
two isoforms
-
-
Manually annotated by BRENDA team
2 forms of enzyme: Mn2+-activated and Mg2+-activated; calf
-
-
Manually annotated by BRENDA team
bovine PAP
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
isoform GLD-2
-
-
Manually annotated by BRENDA team
strain CB15, enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
-
-
Manually annotated by BRENDA team
Coturnix sp.
Quail
-
-
Manually annotated by BRENDA team
CHO fibroblasts
-
-
Manually annotated by BRENDA team
isoform PAP I
-
-
Manually annotated by BRENDA team
pcnB+ and pcnB mutant strains, membrane-associated PAP I is involved in protection of the cell against RNA bacteriophages
-
-
Manually annotated by BRENDA team
strain K12
UniProt
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
UniProt
Manually annotated by BRENDA team
-
Q9BWI3
SwissProt
Manually annotated by BRENDA team
2 forms from nuclear fraction: NE PAP I and II, one form from cytoplasmic fraction: S100 PAP; HeLa cells
-
-
Manually annotated by BRENDA team
2 forms of enzyme: Mn2+-activated, Mg2+-activated; HeLa infected with vaccinia virus
-
-
Manually annotated by BRENDA team
2 forms: 1. nuclear enzyme, stimulated by Mn2+ and Mg2+, 2. cytoplasmic, dependent on Mn2+; HeLa infected with vaccinia virus
-
-
Manually annotated by BRENDA team
HeLa cells
-
-
Manually annotated by BRENDA team
PAP activity is attributed to the protein GLD2
-
-
Manually annotated by BRENDA team
primary breast cancer
-
-
Manually annotated by BRENDA team
CHO fibroblasts
-
-
Manually annotated by BRENDA team
isoform GLD-2
-
-
Manually annotated by BRENDA team
PAP activity is attributed to the protein GLD2
-
-
Manually annotated by BRENDA team
recombinant wild-type and mutant Pap1 were expressed, using the T7 expression system
-
-
Manually annotated by BRENDA team
strain BY4741
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe ATCC 24843
-
UniProt
Manually annotated by BRENDA team
2 forms of enzyme with some difference in primer preference
-
-
Manually annotated by BRENDA team
; positive feedback circuit in which translation of isoform GLD-2 mRNA is stimulated by its polyadenylation, thereby reinforcing the switch to polyadenylate and activate batteries of mRNAs
-
-
Manually annotated by BRENDA team
PAP activity is attributed to the proteins XIGLD-2A and XIGLD-2B
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-, Q9VD44
knockdown of GLD2 transcripts causes male sterility, as GLD2-deficient males do not produce mature sperm. Spermatogenesis up to and including meiosis appears normal in the absence of GLD2, but post-meiotic spermatid development rapidly becomes abnormal. Nuclear bundling and F-actin assembly are defective in GLD2 knockdown testes and nuclei fail to undergo chromatin reorganization in elongated spermatids. GLD2 also affects the incorporation of protamines and the stability of dynamin and transition protein transcripts
physiological function
Q6PIY7
depletion of isoform Gld2 promotes rather than inhibits p53 mRNA polyadenylation/translation, induces premature senescence and enhances the stability of cytoplasmic polyadenylation element binding protein CPEB mRNA. TheCPEB 3' untranslated region contains two miR-122 binding sites, which when deleted, elevate mRNA translation. miR-122 is present in primary fibroblasts and destabilizes by Gld2 depletion; isoform GLD4 regulates p53 polyadenylation/translation in a cytoplasmic polyadenylation element binding protein CPEB dependent manner
physiological function
O17087
removal of either isoform GLD-2 or RNA-binding protein RNP-8 results in shortened poly(A) tails and lowers abundance of four target-mRNAs, i.e. oma-2, egg-1, pup-2, andtra-2. GLD-2 depletion also lowers the abundance of most GLD-2/RNP-8 putative target-mRNAs when assayed on microarrays. The GLD-2/RNP-8 complex is a broad-spectrum regulator of the oogenesis program that acts within an RNA regulatory network to specify and produce fully functional oocytes
physiological function
Q9UTN3
silencing of a few endogenous heterochromatic genes depends on isoform Cid14. The majority of these are subtelomeric genes
physiological function
Schizosaccharomyces pombe ATCC 24843
-
silencing of a few endogenous heterochromatic genes depends on isoform Cid14. The majority of these are subtelomeric genes
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(A)15 + n ATP
(A)15+n + n diphosphate
show the reaction diagram
Q8NDF8
in the presence of ATP, the incorporation of several nucleotides into the RNA substrate is observed
-
-
?
(A)n + ATP
(A)n+1 + diphosphate
show the reaction diagram
P29468
-
-
-
?
(A)n + CTP
(A)n-C + diphosphate
show the reaction diagram
P29468
-
-
-
?
(A)n + diphosphate
(A)n-1 + ATP
show the reaction diagram
P29468
-
-
-
?
(A)n + GTP
(A)n-G + diphosphate
show the reaction diagram
P29468
-
-
-
?
2-aminopurine riboside triphosphate + RNA
?
show the reaction diagram
-
-
-
-
?
adenosine 5'-O-(1-thiotriphosphate) + RNA
diphosphate + ?
show the reaction diagram
-
SP-diastereomer
-
-
?
ATP + 3' untranslated region of mRNA
diphosphate + ?
show the reaction diagram
Q8NDF8
-
-
-
?
ATP + adenosine(5')diphospho(5')adenosine
diphosphate + ?
show the reaction diagram
-
i.e. AP2A
-
-
?
ATP + adenosine(5')pentaphospho(5')adenosine
diphosphate + ?
show the reaction diagram
-
i.e. AP5A
-
-
?
ATP + adenosine(5')tetraphospho(5')adenosine
diphosphate + ?
show the reaction diagram
-
i.e. AP4A
-
-
?
ATP + adenosine(5')triphospho(5')adenosine
diphosphate + ?
show the reaction diagram
-
i.e. AP3A
-
-
?
ATP + AMP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + CMP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + CTP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + dGTP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + GDP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + GTP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + guanosine
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + guanosine(5')diphospho(5')guanosine
diphosphate + ?
show the reaction diagram
-
i.e. GP2G
-
-
?
ATP + guanosine(5')pentaphospho(5')guanosine
diphosphate + ?
show the reaction diagram
-
i.e. GP5G
-
-
?
ATP + guanosine(5')tetraphospho(5')guanosine
diphosphate + ?
show the reaction diagram
-
i.e. GP4G
-
-
?
ATP + guanosine(5')triphospho(5')guanosine
diphosphate + ?
show the reaction diagram
-
i.e. GP3G
-
-
?
ATP + IMP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + oligo(A)n
diphosphate + oligo(A)n+1
show the reaction diagram
Q8NDF8
-
-
-
?
ATP + oligo(U)n
diphosphate + ?
show the reaction diagram
Q8NDF8
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Q9WVP6
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
P29468
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
-
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
O82312
-
-
-
-
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
P0ABF1
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Coturnix sp.
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Q9BWI3
highly specific for ATP
-
-
r
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
highly specific for ATP
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: various E. coli tRNAs or rRNAs
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
chromatin enzyme uses chromosomal RNA as primer, enzyme from nucleoplasm uses poly(A) and hnRNA isolated from chromatin as primer
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primers: poly(U), poly(C), poly(A), not poly(G)
-
-
-
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
elongation of the primer is distributive
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
elongation of the primer is distributive
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: dinucleoside phosphates having 3'-OH
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: viral RNA MS-2 and QB
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no primer: mixture of tRNA, primer: short poly(U)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
Mg2+-activated enzyme from calf thymus or HeLa cells prefers either longer poly(A) or RNAs rather than shorter oligomers of AMP
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Coturnix sp.
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
length of the poly(A) tail is dependent on incubation time and RNA primer concentration
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
polyadenylate sequences of 100-200 AMP residues
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer required
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
enzyme also has cleavage activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
enzyme also has cleavage activity
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
polymerase IIa and IIb utilize a variety of natural and synthetic RNAs as well as DNA as primer
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
enzyme has no ATPase or poly(A) degrading activity
-
-
-
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: poly(G,U)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Vaccinia virus, Coturnix sp.
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no specificity for the 3'-terminal nucleotides
length of the poly(A) tail is dependent on incubation time and RNA primer concentration
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
catalyzes the synthesis of polyadenylate linked to the 3'-hydroxyl end of the terminal nucleoside of an RNA primer
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
enzyme uses all four nucleoside triphosphates
-
-
-
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: tRNA lacking terminal adenosine
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
ATP is utilized 2000-fold more than any other nucleoside triphosphate tested
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no specificity for the 3'-terminal nucleotides when poly(C) and poly(I), but not poly(U), primes poly(A) synthesis with the Mg2+-activated enzyme
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Bos taurus, Vaccinia virus, Coturnix sp.
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: rRNA 16S, E. coli
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
enzyme is unable to catalyze pyrophosphorolysis or phosphorolysis reaction
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
human nuclear enzyme and Vaccinia virus enzyme are able to use both RNA and oligo(A) as primer, human cytoplasmic enzyme is able to use RNA but not oligo(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
enzyme also catalyzes hydrolysis of poly(A)
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: RNA homopolymers
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
does not degrade poly(A) associated with poly(A)*poly(U) helical structure
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
poly(A) and poly(C) minimally effective
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: rRNA 23S, E. coli
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Coturnix sp.
-
adenosine 5'-(beta,gamma-methylene)triphosphate is efficiently polymerized into poly(A) with a polymerase from quail oviduct
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no primer: phage RNA, poly(A) is the most effective primer
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
poly(A) is the most effective primer
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no primer: poly(dT)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
influence of shape and size on priming efficiency
polyadenylate sequences of 100-200 AMP residues
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: oligonucleotides A-A-A-A and A-A-A
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
Mg2+-activated calf thymus enzyme uses poly(A), tRNA, small RNA fragments from calf thymus RNA well, but HeLa 18 and 28S rRNA and MS-1 RNA poorly if at all
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
mitochondrial RNA at least five times more efficiently used than nuclear RNA
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: poly(A)
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: poly(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: poly(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: variety of oligoribonucleotides having free 3'-OH
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: methionyl-tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
minimum effective primer length is 4 to 6 nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Vaccinia virus, Coturnix sp.
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no primer: poly(G), no primer: poly(C)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
no primer: poly(U)
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
primer: dephosphorylated poly(A), tRNA
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
Hs2 complexes have very little PAP activity, Hs2 also displays efficient poly(U) polymerase activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
PAP catalyzes the synthesis of poly(A) tails on the 3'-end of pre-mRNA
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
Escherichia coli K12
P0ABF1
-
-
-
?
ATP + RNA
?
show the reaction diagram
-
overview of biological function
-
-
?
ATP + RNA
?
show the reaction diagram
-
synthetic and hydrolytic activities are functions of the same molecule, the level of adenine nucleotides regulates synthesis and degradation of poly(A), the hydrolytic reaction is responsible for poly(A) shortening or turnover, poly(A) itself is a storage form of adenine nucleotides
-
-
?
ATP + RNA
?
show the reaction diagram
-
processing and activation of stored mRNAs after resumption of development
-
-
-
ATP + RNA
?
show the reaction diagram
-
the enzymatic machinery that catalyzes formation of 3'-ends of polyadenylated mRNAs consists of two distinct factors: a poly(A) polymerase and a cleavage/specificity factor required for the correct cleavage at the poly(A) site of pre-mRNA
-
-
?
ATP + RNA
?
show the reaction diagram
-
2 enzymes participate in the polyadenylation of chromosomal RNA, by a coupled mechanism, the chromatin bound enzyme adds 120-130 adenosine nucleotides to chromosomal RNA, the nucleoplasmic enzyme completes the polyadenylation by adding 80-90 more AMP units to the polyadenylated end
-
-
?
ATP + RNA
?
show the reaction diagram
-
involved in the 3'-end processing of mRNA
-
-
?
ATP + RNA
?
show the reaction diagram
-
involved in the 3'-end processing of mRNA
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
show the reaction diagram
-
in absence of ATP: no activity with 8-Cl-ATP, and 8-amino-ATP results in chain termination, in presence of ATP: polyadenylation of the primer is blocked (inhibited) by 8-amino-ATP and 8-Cl-ATP
-
-
?
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
-
-
-
-
?
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
-
adenine can bind in two different configurations in the PAP active site
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, Q7XJ91, Q7XJ92, Q9LMT2
in the assay ATP is added to a final concentration of 0.25 mM
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
preferentially elongates RNA harbouring poly(A) tails bound by Hfq
-
-
?
ATP + rRNA
diphosphate + ?
show the reaction diagram
Q8NDF8
-
-
-
?
ATP + XTP
diphosphate + ?
show the reaction diagram
-
-
-
-
?
ATP + yeast tRNAiMet
diphosphate + ?
show the reaction diagram
Q8NDF8
in vitro-synthesized yeast tRNAiMet, but not the native tRNA is substrate
-
-
?
CTP + RNA
diphosphate + ?
show the reaction diagram
-
12% of the activity with ATP, adenylyltransferase A
-
-
?
CTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
mRNA of isoform gld-1 + ATP
polyadenylated mRNA of isoform gld-1 + diphosphate
show the reaction diagram
-
reaction catalyzed by enzyme isoform GLD-2
-
-
?
UTP + RNA
diphosphate + RNA(U)n
show the reaction diagram
-
recombinant Cid1 shows a preference for UTP over ATP, the poly(U) polymerase activity of recombinant Cid1 out-competes its PAP activity under physiologically relevant conditions
-
-
?
dATP + RNA
diphosphate + ?
show the reaction diagram
-
15% of the activity with ATP
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
-
additional information
?
-
-
enzyme isoform GLD-2 enhances entry into the meiotic cell cycle at least in part by activating oisoform GLD-1 expression
-
-
-
additional information
?
-
-
enzyme may act in the ooplasm on the progression of metaphase I to metaphase II during oocyte maturation
-
-
-
additional information
?
-
-
the enzyme is responsible for the synthesis of the poly(A) tail at the 3'-end of eukaryotic mRNA
-
-
-
additional information
?
-
-
dATP is not used efficiently by the PAP protein, neither CTP nor UTP is an effective substrate, GTP is used at 6.3% of the rate of ATP
-
-
-
additional information
?
-
-
PAP is a substrate for extracellular signal-regulated kinase
-
-
-
additional information
?
-
-
rRNA fragments and tRNA precursors originating from the internal spacer regions of the rrn operons, in particular, rrnB are abundant poly(A) polymerase targets. Glu tRNA precursors originating from the rrnB and rrnG transcripts exhibit long 3' trailers that are primarily removed by polyribonucleotide nucleotidyltransferase and to a lesser extent by RNase II and poly(A) polymerase. Glu tRNA precursors still harbouring the 5' leader can be degraded by a 3' to 5' quality control pathway involving poly(A) polymerase
-
-
-
additional information
?
-
-
isoform PapD1 can utilize all four nucleotides as substrates, although it is more active with ATP or UTP. the lowest activity is observed with GTP
-
-
-
additional information
?
-
Q8NDF8
isoform PapD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. PAPD5 is active without a protein cofactor. The C terminus of PpaD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate. Incorporation of UTP, GTP, CTP is low and limited to single residues, showing a strong preference of isoform PAPD5 for ATP. No substrates: dNTPs
-
-
-
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
2-aminopurine riboside triphosphate + RNA
?
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
-
-
-
-
?
ATP + RNA
?
show the reaction diagram
-
overview of biological function
-
-
?
ATP + RNA
?
show the reaction diagram
-
synthetic and hydrolytic activities are functions of the same molecule, the level of adenine nucleotides regulates synthesis and degradation of poly(A), the hydrolytic reaction is responsible for poly(A) shortening or turnover, poly(A) itself is a storage form of adenine nucleotides
-
-
?
ATP + RNA
?
show the reaction diagram
-
processing and activation of stored mRNAs after resumption of development
-
-
-
ATP + RNA
?
show the reaction diagram
-
the enzymatic machinery that catalyzes formation of 3'-ends of polyadenylated mRNAs consists of two distinct factors: a poly(A) polymerase and a cleavage/specificity factor required for the correct cleavage at the poly(A) site of pre-mRNA
-
-
?
ATP + RNA
?
show the reaction diagram
-
2 enzymes participate in the polyadenylation of chromosomal RNA, by a coupled mechanism, the chromatin bound enzyme adds 120-130 adenosine nucleotides to chromosomal RNA, the nucleoplasmic enzyme completes the polyadenylation by adding 80-90 more AMP units to the polyadenylated end
-
-
?
ATP + RNA
?
show the reaction diagram
-
involved in the 3'-end processing of mRNA
-
-
?
ATP + RNA
?
show the reaction diagram
-
involved in the 3'-end processing of mRNA
-
-
?
additional information
?
-
-
enzyme isoform GLD-2 enhances entry into the meiotic cell cycle at least in part by activating oisoform GLD-1 expression
-
-
-
additional information
?
-
-
enzyme may act in the ooplasm on the progression of metaphase I to metaphase II during oocyte maturation
-
-
-
additional information
?
-
-
the enzyme is responsible for the synthesis of the poly(A) tail at the 3'-end of eukaryotic mRNA
-
-
-
additional information
?
-
-
rRNA fragments and tRNA precursors originating from the internal spacer regions of the rrn operons, in particular, rrnB are abundant poly(A) polymerase targets. Glu tRNA precursors originating from the rrnB and rrnG transcripts exhibit long 3' trailers that are primarily removed by polyribonucleotide nucleotidyltransferase and to a lesser extent by RNase II and poly(A) polymerase. Glu tRNA precursors still harbouring the 5' leader can be degraded by a 3' to 5' quality control pathway involving poly(A) polymerase
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
interaction with Xenopus CPEB in vitro
-
additional information
-
interaction with cytoplasmic polyadenylation factors, including CPSF and CPEB, and with target mRNAs
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
KCl
-
maximal stimulation at 40 mM, inhibition above 250 mM
KCl
-
maximal activity at 33 mM, inhibition above 150 mM
KCl
-
requirement is dependent on the primer and the divalent cation used
KCl
-
optimal concentration: 60 mM
Mg2+
-
ATP is utilized 150-fold more with Mn2+ than with Mg2+
Mg2+
-
one-fifth of the activity of Mg2+ in NTP activation
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
10% of the activity with Mn2+
Mg2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mg2+
-
Vaccinia virus enzyme is stimulated by Mn2+ and also by Mg2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
Mg2+ is inactive, maximum activity in presence of both Mn2+ and Mg2+
Mg2+
-
NE PAP I (isoenzyme from cytoplasmic fraction) and S100 PAP (isoenzyme from nuclear fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
Mg2+
-
in presence of Mg2+ and a specificity factor required for correct cleavage at the poly(A) site of pre-mRNA; more active in presence of Mn2+ than Mg2+
Mg2+
-
more active in presence of Mn2+ than Mg2+; optimal concentration: 4-6 mM
Mg2+
-
more active in presence of Mn2+ than Mg2+; optimal concentration depends on ATP concentration
Mg2+
-
in presence of Mg2+ and a specificity factor required for correct cleavage at the poly(A) site of pre-mRNA
Mg2+
-
optimal concentration: 8-10 mM, polymerase I from chromatin, polymerase II from nucleoplasm is inactive in presence of Mg2+
Mg2+
-
-
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
Mg2+ or Mn2+ required; optimal concentration: 5 mM
Mg2+
-
completely inactive in presence of Mg2+
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
-
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
optimal concentration is about 5 mM
Mg2+
-
essential for activity
Mg2+
-
Mg2+ ions can release the inhibition of PAPgamma by aminoglycosides
Mg2+
-
required for activity
Mg2+
-
or Mn2+, required
Mn2+
-
ATP is utilized 150-fold more with Mn2+ than with Mg2+
Mn2+
-
required for NTP activation
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
required
Mn2+
-
more active in presence of Mg2+ than Mn2+
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
absolute requirement; optimal concentration: 0.25-0.75 mM
Mn2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mn2+
-
Vaccinia virus enzyme is stimulated by Mn2+ and also by Mg2+
Mn2+
-
Mg2+ can partially replace Mn2+ in the reaction with polymerase II; required
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
more active in presence of Mn2+ than Mg2+; optimal concentration: 0.50-0.75 mM
Mn2+
-
more active in presence of Mn2+ than Mg2+; optimal concentration: 0.25-1.0 mM; required
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
maximum activity in presence of both Mn2+ and Mg2+; optimal concentration: 4 mM (polymerase IIa), 4-8 mM (polymerase IIb)
Mn2+
-
exclusively activated by Mn2+
Mn2+
-
NE PAP I (isoenzyme from nuclear fraction) and S100 PAP (isoenzyme from cytoplasmic fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
Mn2+
-
more active in presence of Mn2+ than Mg2+; optimal concentration: 0.5 mM (at 0.5 mM ATP)
Mn2+
-
more active in presence of Mn2+ than Mg2+; optimal concentration depends on ATP concentration
Mn2+
-
nonspecific adenylation of RNA in presence of Mn2+
Mn2+
-
optimal concentration: 2 mM; required
Mn2+
-
optimal concentration: 2-4 mM; required
Mn2+
-
optimal concentration: 0.8 mM (polymerase I and II)
Mn2+
-
-
Mn2+
-
more active in presence of Mg2+ than Mn2+
Mn2+
-
Mn2+ or Mg2+ required; optimal concentration: 2 mM
Mn2+
-
required
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
more active in presence of Mg2+ than Mn2+
NH4+
-
maximal activity at 33 mM, inhibition above 150 mM
Mn2+
-
or Mg2+, required
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
low ionic strength required for maximal activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
1 mM, 28% inhibition, major poly(A) polymerase, 50% inhibition, minor poly(A) polymerase
3'-Acetyl-1'-benzyl-2'-methylpyrrolo[3,2-C]4-deoxyrifamycin
-
-
3-(4-Benzyl-2,6-dimethyl piperazinoiminomethyl)rifamycin SV
-
-
3-(4-Ethylpiperazinoiminomethyl) rifamycin SV
-
-
5-epi-sisomycin
-
pH-dependent inhibition, non-competitive inhibitor for ATP
8-amino-ATP
-
C-8 substitution influences sugar pucker conformation, which may affect yPAP efficiently
-
8-aza-ATP
-
slight inhibition
8-azido-ATP
-
slight inhibition
8-bromo-ATP
-
halogen modification at C-8 may negatively affect the ability of the enzyme to activate the ATP substrate or to transfer the AMP group from the enzyme to the RNA substrate
8-chloro-ATP
-
-
-
adenosine 5'-(alpha,beta-methylenetriphosphate)
-
-
adenylyl-(3'-5')adenosine
-
-
Adenylyl-(3'-5')cytosine
-
-
ADP
-
inhibits hydrolytic reaction
alpha, beta-methylene-ATP
-
a nonreactive ATP analogue
alpha-Amanitin
-
-
AMP
-
inhibits hydrolytic reaction
ATP
-
hepatoma enzyme less effective to substrate inhibition than liver enzyme
ATP
-
inhibits hydrolytic reaction
ATP
-
above 0.5 mM
aurintricarboxylic acid
-
-
Bentonite
-
-
-
CaCl2
-
remaining activity 3%
Calf thymus DNA
-
-
-
CoCl2
-
remaining activity 75%
cordycepin
-
not
cordycepin
-
not
Cordycepin 5'-triphosphate
-
-
Cordycepin triphosphate
-
5.0 mM
CuCl2
-
remaining activity 0.1%
dATP
-
0.25 mM, 50% inhibition, major poly(A) polymerase, 15% inhibition, minor poly(A) polymerase
diphosphate
-
noncompetitive to ATP and primer
diphosphate
-
-
diphosphate
-
-
diphosphate
-
product inhibitor
EDTA
-
100% inhibition at 0.5 mM
GMP
-
1 mM, complete inhibition of enzymic reaction with tRNA
heparin
-
-
hygromycin B
-
pH-dependent inhibition
Ionic strength
-
-
-
K+
-
100 mM; KCl
K+
-
KCl; maximal stimulation at 40 mM, inhibition above 250 mM
K+
-
above 50 mM; KCl
K+
-
80 mM: 50% inhibition; KCl
kanamycin A
-
pH-dependent inhibition
kanamycin B
-
pH-dependent inhibition
KCl
-
stimulation at low concentrations, at 300 mM, 15% inhibition, major poly(A) polymerase, 52% inhibition, minor poly(A) polymerase
lividomycin A
-
pH-dependent inhibition
N-ethylmaleimide
-
inhibits Mn2+-activated enzyme
N-ethylmaleimide
-
-
N-ethylmaleimide
-
inhibits Mn2+-activated enzyme
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
Na+
-
0.1 M; NaCl
Na2HPO4
-
-
Na2HPO4
-
dibasic sodium phosphate
NaF
-
10 mM, complete inhibition
neomycin B
-
an increase in pH releases the neomycin B inhibitory effect on PAPgamma
NH4+
-
10-40 mM; ammonium sulfate
NH4+
-
0.1 M polymerase Ia and Ib completely inhibited, polymerase II: 68% inhibition; ammonium sulfate
NH4+
-
ammonium sulfate; maximal activity at 33 mM, inhibition above 150 mM
NH4+
-
50 mM: 50% inhibition; ammonium sulfate
Pancreatic ribonuclease
-
-
-
paromomycin
-
pH-dependent inhibition
PD98059
-
induces partial inhibition of PAP phosphorylation at S537
phosphate
-
-
phosphate
-
not: rat liver nuclear enzyme
PO43-
-
not inhibitory
Polyamines
-
-
-
Polyphosphate
-
inhibition depends on chain length, P3 10% at 0.001 mM, P4 60% at 0.001 mM, P15 90% at 0.001 mM, P35 100% at 0.001 mM
Polyphosphate
-
with 20 nM to 0.002 mM of polyphosphate the length of the products is reduced but inhibition is not complete
Polyphosphate
-
potent inhibitor of poly(A) polymerase activity, almost complete inhibition at 200 nM
Polyvinyl sulfate
-
-
putrescine
-
-
-
Ribonucleoside triphosphates other than ATP
-
-
ribostamycin
-
pH-dependent inhibition
Rifampicin
-
not inhibitory
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
Rifamycin B:N,N-diethylamide
-
-
Rifamycin B:N,N-dipentylamide
-
-
Rifamycin derivatives
-
some derivatives are effective, others not
-
rifamycin SV
-
-
sisomicin
-
pH-dependent inhibition, non-competitive inhibitor for ATP
small ubiquitin-like modifier
-
in vitro sumoylation inhibits the activity of purified PAP
-
Sodium vanadate
-
-
spermine
-
inhibition if poly(A), nuclear RNA, or tRNA serves as primer, not with short oligonucleotide primers such as (Ap)3A
tobramycin
-
pH-dependent inhibition
Zn2+
-
inhibits PAP activity at concentrations above 10 M in the presence of 5 mM MgCl2
Mn2+
-
high concentrations
additional information
-
not inhibitory: actinomycin D; not inhibitory: alpha-amanitin
-
additional information
-
insensitive to high levels of RNA-polymerase inhibitors
-
additional information
-
not inhibitory: alpha-amanitin
-
additional information
-
not inhibitory: alpha-amanitin
-
additional information
-
not inhibitory: alpha-amanitin
-
additional information
-
not inhibitory: 3-formalrifamycin SV:o-methyloxime; not inhibitory: 4-(dimethylamino)-4-deoxyrifamycin SV
-
additional information
-
not inhibitory: rifampicin, streptolydigin, phosphate at 0.5 mM, cordycepin at 0.1 mM
-
additional information
-
stem-loop structure in mRNA 3-ends may be inhibitory
-
additional information
-
Fip1, a component of yeast polyadenylation factor I, has an inhibitory effect on the enzyme activity because it competes with RNA for access to the C-RBS region
-
additional information
-
cytoplasmic polyadenylation elements and PUF-binding elements are required for repression of GLD-2 mRNA
-
additional information
-
Fippbd peptide does not inhibit Pap1 activity even at concentrations in excess of 0.2 mM
-
additional information
-
not inhibited by neamine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3',5'-AMP
-
slight stimulation
Dinucleotide
-
in presence of 0.5 mM ATP, activation in decreasing order: GP4G, GP3G, AP6A, GP2G, AP4A, AP2A, GP5G, AP5A, AP3A, activation at 0.01 mM is 4-10fold
dithiothreitol
-
required
germ cell-specific gene 1 protein
Q9WVP6
TPAP interaction partner protein leading to redistribution of TPAP from the cytosol to the endoplasmic reticulum
-
host factor I
-
Hfq-PAP I interaction facilitates RNA recognition by PAP I
-
phosphatidylinositol 4,5-bisphosphate
-
in the presence of 50 mM phosphatidylinositol 4,5-bisphosphate Star-PAP activity is markedly stimulated
Poly(U)
-
stimulates
spermidine
-
slight stimulation, 5 mM
KCl
-
major poly(A) polymerase, optimal at 250 mM, minor poly(A) polymerase, optimal at 125 mM, inhibition of both above 250 mM
additional information
-
the enzyme is kept inactive in the G complex prior to the onset of meiotic maturation. Activation could involve the removal of inhibitory modifications of GLD2
-
additional information
-
other phosphoinositides besides phosphatidylinositol 4,5-bisphosphate do not affect Star-PAP activity, and no phosphoinositide has an effect on PAPalpha activity
-
additional information
-
PAP phosphorylation of serine 537 by extracellular signal-regulated kinase increases its nonspecific polyadenylation activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00092
-
(A)15
Q8NDF8
wild-type, pH 7.5, 37C
-
0.00319
-
(A)15
Q8NDF8
mutant K560E, pH 7.5, 37C
-
0.00534
-
(A)15
Q8NDF8
C-terminal deletion mutant, pH 7.5, 37C
-
0.0468
-
(A)n
-
wild-type, pH 7.0, 30C
0.106
-
(A)n
-
mutant N189A, pH 7.0, 30C
0.195
-
(A)n
-
mutant K215A, pH 7.0, 30C
0.367
-
(A)n
-
mutant N226A, pH 7.0, 30C
0.711
-
(A)n
-
mutant Y224F, pH 7.0, 30C
0.0197
-
2-aminopurine riboside triphosphate
-
-
0.028
-
ATP
-
37C, pH 8.0
0.03
-
ATP
-
polymerase IIa, 37C
0.031
-
ATP
-
mutant Y224S
0.036
-
ATP
-
wild-type, pH 7.0, 30C
0.039
-
ATP
-
30C, pH 8.0
0.04
-
ATP
-
30C, pH 8.5
0.04
-
ATP
-
wild-type PAP
0.0469
-
ATP
Q8NDF8
mutant K560E, pH 7.5, 37C
0.047
-
ATP
-
pH 8.0, 37C
0.05
-
ATP
-
p(A)3 primer, Mn2+-activated calf thymus enzyme
0.05
-
ATP
-
oligoadenylate (in presence of Mn2+)
0.05
-
ATP
-
polymerase IIb, 37C
0.05
-
ATP
-
30C, pH 8.0
0.06
-
ATP
-
mutant Y224F
0.062
-
ATP
-
mutant N226A
0.0636
-
ATP
Q8NDF8
wild-type, pH 7.5, 37C
0.0643
-
ATP
Q8NDF8
C-terminal deletion mutant, pH 7.5, 37C
0.07
-
ATP
-
37C, pH 8.0
0.08
-
ATP
-
mutant N189A, pH 7.0, 30C
0.086
-
ATP
-
pH 8.0, 37C
0.096
-
ATP
-
mutant K215A
0.123
-
ATP
-
incubation at 30 C for 15 min, using oligo(A)17C (a modification of the 3'-terminal residue from A to C)
0.13
-
ATP
-
incubation 30 min at 30 C
0.136
-
ATP
-
mutant D167N
0.143
-
ATP
-
major poly(A) polymerase, 37C, pH 8.0
0.15
-
ATP
-
37C, pH 8.0
0.154
-
ATP
-
mutant D167N/N202A
0.207
-
ATP
-
mutant N239A
0.213
-
ATP
-
mutant F153A
0.229
-
ATP
-
wild-type, reactions are started with the addition of PAP and incubated at 37 C for 15 minutes. Reactions are stopped by the addition of 8 microL of stop buffer (formamide with trace amount of bromophenol blue dye)
0.232
-
ATP
-
mutant V156A
0.247
-
ATP
-
mutant A319R
0.248
-
ATP
-
mutant K158A
0.249
-
ATP
-
mutant N226A, pH 7.0, 30C
0.255
-
ATP
-
mutant R199A
0.256
-
ATP
-
mutant V154A
0.266
-
ATP
-
mutant V247A
0.275
-
ATP
-
mutant N202A
0.297
-
ATP
-
mutant V247R
0.298
-
ATP
-
mutant Q323A
0.308
-
ATP
-
37C, pH 8.0
0.357
-
ATP
-
mutant V206A
0.361
-
ATP
-
mutant F100D
0.4
-
ATP
-
major poly(A) polymerase, 37C, pH 8.0
0.406
-
ATP
-
mutant K215A, pH 7.0, 30C
0.503
-
ATP
-
mutant K232A
0.627
-
ATP
-
mutant D167N/T317G
0.929
-
ATP
-
mutant Y224F, pH 7.0, 30C
1.002
-
ATP
-
mutant T317G
1.402
-
ATP
-
mutant Y237A
2.191
-
ATP
-
mutant K228A
0.104
-
CTP
-
wild-type, pH 7.0, 30C
0.14
-
CTP
-
mutant N226A, pH 7.0, 30C
0.148
-
CTP
-
mutant N189A, pH 7.0, 30C
0.27
-
CTP
-
incubation 30 min at 30 C
0.368
-
CTP
-
mutant K215A, pH 7.0, 30C
4.7
-
CTP
-
mutant Y224F, pH 7.0, 30C
0.06
-
dATP
-
30C, pH 8.5
0.055
-
GTP
-
mutant N226A, pH 7.0, 30C
0.01
-
oligo(A)
-
Mn2+-activated enzyme, pH 8.3, 37C
0.3
-
oligo(A)
-
Mg2+-activated enzyme, pH 8.3, 37C
0.00039
-
oligo(A)12
-
incubation 30 min at 30 C
-
0.0005
-
oligo(A)14
-
wild-type PAP, incubation at 30 C
-
0.006
-
oligo(A)14
-
mutant Y224S
-
0.015
-
oligo(A)14
-
mutant Y224F
-
0.028
-
oligo(A)14
-
mutant N226A
-
0.037
-
oligo(A)14
-
mutant K215A
-
0.0263
-
oligo(A)17C
-
incubation at 30 C for 15 min in the presence of MgATP2-
-
0.0468
-
oligo(A)18
-
incubation at 30 C for 15 min in the presence of MgATP2-
-
0.0642
-
oligo(A)18
-
incubation at 30 C for 15 min in the presence of MgCTP2-
-
0.2
-
oligoadenylate
-
in presence of Mg2+, pH 9.0, 35C
0.0036
-
Poly(A)
-
Mn2+-activated enzyme, pH 8.3, 37C
0.14
0.36
Poly(A)
-
Mg2+-activated enzyme, pH 8.3, 37C
0.51
-
RNA (A)15
-
mutant A319R
-
0.74
-
RNA (A)15
-
mutant K232A
-
1.34
-
RNA (A)15
-
wild-type
-
1.43
-
RNA (A)15
-
mutant K228A
-
1.47
-
RNA (A)15
-
mutant V154A
-
1.88
-
RNA (A)15
-
mutant Q323A
-
2.63
-
RNA (A)15
-
mutant Y237A
-
2.8
-
RNA (A)15
-
mutant V206A
-
3.13
-
RNA (A)15
-
mutant T317G
-
5.31
-
RNA (A)15
-
mutant K158A
-
6.94
-
RNA (A)15
-
mutant N239A
-
7.32
-
RNA (A)15
-
mutant V156A
-
9.85
-
RNA (A)15
-
mutant V247A
-
10.21
-
RNA (A)15
-
mutant R199A
-
11.16
-
RNA (A)15
-
mutant V247R
-
11.44
-
RNA (A)15
-
mutant N202A
-
12.72
-
RNA (A)15
-
mutant G203H
-
13.15
-
RNA (A)15
-
mutant D167N
-
14.37
-
RNA (A)15
-
mutant F100D
-
16.41
-
RNA (A)15
-
mutant D167N/N202A
-
18.82
-
RNA (A)15
-
mutant D167N/T317G
-
22.84
-
RNA (A)15
-
mutant D167N/V247R
-
24.99
-
RNA (A)15
-
mutant F153A
-
0.002
-
RNA primer
-
-
-
0.007
-
short poly(A)
-
-
0.062
-
GTP
-
wild-type, pH 7.0, 30C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
dependence on divalent cation concentration
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.142
-
(A)15
Q8NDF8
mutant K560E, pH 7.5, 37C
-
0.147
-
(A)15
Q8NDF8
C-terminal deletion mutant, pH 7.5, 37C
-
0.18
-
(A)15
Q8NDF8
wild-type, pH 7.5, 37C
-
0.002
-
ATP
-
mutant V247R
0.006
-
ATP
-
mutant D167N/N202A
0.007
-
ATP
-
mutant D167N/T317G
0.009
-
ATP
-
mutant D167N
0.015
-
ATP
-
mutant F100D
0.018
-
ATP
-
mutant V156A
0.022
-
ATP
-
mutant N202A
0.027
-
ATP
Q8NDF8
C-terminal deletion mutant, pH 7.5, 37C
0.028
-
ATP
Q8NDF8
mutant K560E, pH 7.5, 37C
0.097
-
ATP
Q8NDF8
wild-type, pH 7.5, 37C
0.098
-
ATP
-
mutant R199A
0.308
-
ATP
-
mutant F153A
0.82
-
ATP
-
mutant K158A
1.055
-
ATP
-
mutant N239A
1.073
-
ATP
-
mutant Y237A
1.15
-
ATP
-
mutant K228A
1.24
-
ATP
-
mutant V154A
1.25
-
ATP
-
mutant T317G
1.411
-
ATP
-
mutant V247A
1.476
-
ATP
-
mutant K232A
3.19
-
ATP
-
mutant V206A
4.203
-
ATP
-
wild-type, reactions are started with the addition of PAP and incubated at 37 C for 15 minutes. Reactions are stopped by the addition of 8 microL of stop buffer (formamide with trace amount of bromophenol blue dye)
4.88
-
ATP
-
mutant Q323A
6.092
-
ATP
-
mutant A319R
30
-
ATP
-
cosubstrates rA(pA)5, pH 9.0, 35C
0.43
-
CTP
-
incubation 30 min at 30 C
3.33
-
Nucleotide
-
-
0.0025
-
RNA(A)15
-
mutant D167N/V247R
-
0.006
-
RNA(A)15
-
mutant G203H
-
0.08
-
RNA(A)15
-
mutant N202A
-
0.1
-
RNA(A)15
-
mutant D167N/N202A
-
0.18
-
RNA(A)15
-
mutant V247R
-
0.26
-
RNA(A)15
-
mutant D167N/T317G
-
0.39
-
RNA(A)15
-
mutant V156A
-
0.67
-
RNA(A)15
-
mutant F100D
-
0.82
-
RNA(A)15
-
mutant R199A
-
1.43
-
RNA(A)15
-
mutant D167N
-
6.76
-
RNA(A)15
-
mutant K228A
-
6.86
-
RNA(A)15
-
mutant T317G
-
8.18
-
RNA(A)15
-
mutant K158A
-
10.52
-
RNA(A)15
-
mutant F153A
-
11.37
-
RNA(A)15
-
mutant N239A
-
12.58
-
RNA(A)15
-
mutant V206A
-
19.25
-
RNA(A)15
-
mutant Y237A
-
19.71
-
RNA(A)15
-
mutant Q323A
-
20.34
-
RNA(A)15
-
mutant K232A
-
22.75
-
RNA(A)15
-
mutant A319R
-
22.78
-
RNA(A)15
-
wild-type
-
28.96
-
RNA(A)15
-
mutant V154A
-
34.5
-
RNA(A)15
-
mutant V247A
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
27.5
-
(A)15
Q8NDF8
C-terminal deletion mutant, pH 7.5, 37C
0
44.4
-
(A)15
Q8NDF8
mutant K560E, pH 7.5, 37C
0
195.7
-
(A)15
Q8NDF8
wild-type, pH 7.5, 37C
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0004
0.0006
3'-dATP
-
30C, pH 8.0
0.0063
-
3'-dATP
-
incubation at 37 C for 20 min
0.6
1
3'-dATP
-
-
0.0019
-
8-amino-ATP
-
incubation at 37 C for 20 min
-
4
10
Poly(dT)
-
-
0.0002
-
polyphosphate P15
-
competitive, 30C, pH 7.0
-
0.0005
-
polyphosphate P4
-
competitive, 30C, pH 7.0
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0939
-
-
30C, pH 8.4
28.33
-
-
35C, pH 9.0
3175
-
-
37C, pH 8.3
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-, Q7XJ91, Q7XJ92, Q9LMT2
ca. 17,000 U/mg Protein; ca. 17,000 U/mg Protein; ca. 17,000 U/mg Protein
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.4
8
-
in presence of Mn2+
7
-
-
Mn2+-activated enzyme
8
8.5
-
-
8
-
-
vaccinia virus enzyme, human, cytoplasmic Mn2+-dependent enzyme
8
-
-
polymerase IIa and IIb
8
-
-
Mg2+-activated enzyme
8
-
-
polymerase II (nucleoplasm)
8.3
-
-
-
8.3
-
-
human nuclear Mn2+- and Mg2+-activated enzyme
8.3
-
-
Mn2+-activated enzyme
8.5
-
-
polymerase I (chromatin)
9.5
-
-
adenylyltransferase A
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
pH 6: 47% (polymerase IIa) and 5% (polymerase IIb) of maximum activity, pH 9: 55% of maximum activity
7
8.5
-
pH 7: about 40% of maximum activity, pH 8-8.5: maximum activity
7
8.8
-
about 50% of maximum activity at pH 7.0 and pH 8.8
7
9
-
about 65% of maximum activity at pH 7.0 and pH 9.0
7.2
9.2
-
pH 7.2: 55% of maximum activity, pH 9.2: 62% of maximum activity
7.5
9
-
pH 7.5: 50% of maximum activity, pH 9.0: 15% of maximum activity
8
10
-
pH 8: about 40% of maximum activity, pH 10: about 50% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the protein level is relatively low in the brain
Manually annotated by BRENDA team
-
encysted, dormant
Manually annotated by BRENDA team
Q6PIY7
primary foreskin fibroblasts
Manually annotated by BRENDA team
-, Q7XJ91, Q7XJ92, Q9LMT2
-
Manually annotated by BRENDA team
-
cryptobiotic gastrula
Manually annotated by BRENDA team
-
the protein level is relatively low in the heart
Manually annotated by BRENDA team
-
infected with vaccinia virus
Manually annotated by BRENDA team
-
Morris hepatoma tumor cells 3924A
Manually annotated by BRENDA team
-
Morris hepatomas 3924A and 7777, relative lack of poly(A) polymerase activity is partly due to decreased level of this enzyme in the tumors, but largely due to the nonavailability of the primer-binding sites on the solubilized enzyme and to occupation of the available binding sites with an ineffective primer
Manually annotated by BRENDA team
-, Q7XJ91, Q7XJ92, Q9LMT2
-
Manually annotated by BRENDA team
-
mRNA is present in meiotically maturing oocyte, protein is present only at the metaphases I and II after germinal vesicle breakdown
Manually annotated by BRENDA team
Coturnix sp.
-
-
Manually annotated by BRENDA team
-, Q7XJ91, Q7XJ92, Q9LMT2
-
Manually annotated by BRENDA team
-
germinating embryo
Manually annotated by BRENDA team
-
the protein level is relatively low in the spleen
Manually annotated by BRENDA team
-, Q7XJ91, Q7XJ92, Q9LMT2
-
Manually annotated by BRENDA team
-, Q9VD44
expression in testis, localizes to elongating spermatogenic cysts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
PAP I leader sequence directs the protein to the cellular membrane
-
Manually annotated by BRENDA team
-
infected cytoplasm of HeLa cells
Manually annotated by BRENDA team
-
2 forms from nuclear fraction: NE PAPs I and II, one form from cytoplasmic fraction: S100 PAP
Manually annotated by BRENDA team
-
of somatic, testicular, and cultured cells
Manually annotated by BRENDA team
-
Gld-2 is localized in the cytoplasm of oocytes at the metaphases I and II, Tpap is localized predominantly in the cytoplasm of pachytene spermatocytes and round spermatids
Manually annotated by BRENDA team
-
2 forms from nuclear fraction: NE PAPs I and II, one form from cytoplasmic fraction: S100 PAP
Manually annotated by BRENDA team
-
2 forms: one from chromatin and one from nucleoplasm
Manually annotated by BRENDA team
-
of somatic, testicular, and cultured cells
Manually annotated by BRENDA team
-
Gld-2 is predominantly localized in the nucleus
Manually annotated by BRENDA team
-
sumoylation is required to facilitate PAP nuclear localization
Manually annotated by BRENDA team
additional information
-
plasmid
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
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)
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)
Vaccinia virus (strain Western Reserve)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37000
-
-
gel filtration, minor poly(A) polymerase
43000
-
-
polymerase Ia and Ib, gel filtration
45000
60000
-
sedimentation analysis
47000
-
-
gel filtration
50000
60000
-
enzymes NE PAP I and II, S100 PAP, sucrose density gradient sedimentation
50000
60000
-
gel filtration
54000
-
-
Gld-2
57000
-
-
and 60000, 2 major forms of enzyme, gel filtration
57000
-
-
glycerol density gradient centrifugation
58000
-
-
-
58000
-
-
Mg2+-activated enzyme, sedimentation analysis
58000
-
-
nuclear Mg2+- and Mn2+-stimulated enzyme, glycerol density gradient sedimentation
58000
-
-
gel filtration
58000
-
-
adenylyltransferase B, glycerol density gradient sedimentation
60000
-
-
Mn2+-activated enzyme, sedimentation analysis, gel filtration
60000
-
-
mitochondria, glycerol density gradient centrifugation
60000
-
-
and 57000, 2 major forms of enzyme, gel filtration
62000
-
-
-
62000
-
-
sucrose density gradient sedimentation, gel filtration
63000
-
-
Mn2+-activated, sedimentation analysis
63000
-
-
cytoplasmic Mn2+-dependent enzyme, glycerol density gradient sedimentation
65000
70000
-
gel filtration
65000
-
-
embryo, sedimentation analysis, gel filtration
70000
-
-
enzyme from infected cytoplasm, glycerol density gradient sedimentation
70000
-
-
gel filtration
76990
-
-
predicted from nucleotide sequence
80000
-
-
sucrose density gradient sedimentation
80000
-
-
sucrose density gradient sedimentation
82400
-
-
predicted from nucleotide sequence
86000
-
-
gel filtration, major poly(A) polymerase
95000
-
-
polymerase II, gel filtration
100000
-
-
SDS-PAGE
120000
140000
-
Mg2+-activated enzyme, gel filtration
120000
-
-
gel filtration
140000
160000
-
gel filtration
145000
155000
-
gel filtration
145000
-
-
polymerase IIa, gel filtration
150000
-
-
above, mouse L-cells, gel filtration
155000
-
-
polymerase IIb, gel filtration
180000
-
-
corresponds to the PAP protein encoded by gene CG15737, SDS-PAGE
185000
-
-
adenylyltransferase A, glycerol density gradient sedimentation
200000
-
-
small ubiquitin-like modifier-2/3-modified forms of PAP, SDS-PAGE
additional information
-
-
heterogenous, monomers to very large aggregates, all forms being active, gel filtration, recombinant protein
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 50000, denaturing gel electrophoresis
?
-
x * 50000, Mg2+-activated, denaturing gel electrophoresis; x * 75000, Mn2+-activated, denaturing gel electrophoresis
?
-
x * 48000, rat liver nucleoplasm, denaturing gel electrophoresis; x * 60000, hepatoma enzyme, SDS-PAGE
?
-
x * 63000, SDS-PAGE
?
-
x * 48000, liver enzyme, SDS-PAGE; x * 60000, hepatoma enzyme, SDS-PAGE
?
-
x * 70000, SDS-PAGE
?
-
x * 50000, heterogenous, monomers to very large aggregates, all forms being active, SDS-PAGE, gel filtration, recombinant protein
?
-
x * 80000, SDS-PAGE
?
Q9BWI3
x * 83000, SDS-PAGE, x * 82800, deduced from gene sequence
?
-
x * 85000, SDS-PAGE, recombinant enzyme
?
-
x * 54000, SDS-PAGE
dimer
-
1 * 51000 + 1 * 35000, SDS-PAGE
dimer
-
1 * 37000 + 1 * 57000, SDS-PAGE
dimer
-
1 * 85000 + 1 * 60000, SDS-PAGE
heterodimer
-
a distinct RNA-binding protein, GLD-3, binds to GLD-2 and stimulates its polyadenylation activity in vitro
heterotrimer
-
the large PAP subunit AMV038 functions alone to produce short poly(A) tails, the small PAP-subunit AMV060 exhibits 2'-O-methyltransferase activity
monomer
-
1 * 60000, Mn2+-activated enzyme, denaturing gel electrophoresis
monomer
-
1 * 62000, SDS-PAGE
monomer
-
1 * 50000, nuclear Mn2+- and Mg2+-activated enzyme, SDS-PAGE; 1 * 75000, cytoplasmic, Mn2+-dependent enzyme, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 64000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE
monomer
-
1 * 63000, SDS-PAGE
monomer
-
1 * 64000, SDS-PAGE
tetramer
-
4 * 30000, SDS-PAGE
monomer
-
1 * 57000, SDS-PAGE
additional information
-
enzyme interacts directly with cleavage factor I, implications for assembly of the processing complex and regulation of enzyme
additional information
-
binding of enzyme to nuclear poly(A) binding protein results in 80-fold increase in apparent affinity for RNA, mechanism
additional information
-
polynucleotide adenylyltransferase Trf5p is part of a complex similar to TRAMP complex and with overlapping functions
additional information
-
Pap1 N-terminus interacts with the first 300 amino acids of Pta1 and with Cft1, two subunits of the cleavage/polyadenylation factor, in which Pap1 resides, and with nucleic-acid binding proteins Nab6 and Sub1with known links to 30 end processing
additional information
-
dimerization is required for the catalytic activity of isoform PAPD1
additional information
Q9UTN3
isoform Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14-Air1 complex. Helicase Mtr4, Cid14, and Air1 form a TRAMP-like complex. Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors.No physical link to chromatin has been identified
additional information
Schizosaccharomyces pombe ATCC 24843
-
isoform Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14-Air1 complex. Helicase Mtr4, Cid14, and Air1 form a TRAMP-like complex. Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors.No physical link to chromatin has been identified
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
sumoylation
-
posttranslational sumoylation is required to facilitate PAP nuclear localization and enhances PAP stability
glycoprotein
-
-
glycoprotein
-
-
additional information
-
not glycosylated
phosphoprotein
-
enzyme PAP I variant with C-terminal His-tag can be phosphorylated both in vivo and in vitro. In vivo phosphorylation impairs activity of the enzyme and may be a regulatory process
additional information
Q9BWI3
no phosphoprotein
additional information
-
sequence contains an N-terminal signal of 17 amino acids for localization to the nucleus
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Crystals of PAP complexed to 3'-dATP and Mn2+ are grown from a solution made of 22% (w/v) polyethylene glycol 8000, 100 mM Mes (pH 6), 120 mM ammonium sulfate, 5 mM CaCl2, 2 mM MnCl2, and 2 mM beta-mercaptoethanol. Cocrystallization of PAP with 3'-dATP and MgCl2 is performed under conditions similar to those reported, with the exception that 5 mM MgCl2 is used instead of 2 mM MnCl2. Crystals are of the space group p212121, with one monomer per asymmetric unit and a solvent content of ~55%.
-
in complex with an ATP analog
-
mutant C36S/C118V/A152C/C160S/C197S/C257S/C293S/C204V in complex with a chemically modified RNA, to 2.25 A resolution
-
mutant D325A, to 3.1 A resolution. The overall structure of the palm and fingers domains is similar to that in the canonical poly(A) polymerases. The active site is located at the interface between the two domains, with a large pocket that can accommodate the substrates. The structure reveals a domain in the N-terminal region of PAPD1, with a backbone-fold that is similar to that of RNP-type RNA binding domains. This domain, together with a beta-arm insertion in the palm domain, contributes to dimerization of PAPD1. The crystal structure reveals a dimer, formed by the two molecules in the asymmetric unit
-
alone and in complex with 3-dATP
-
hanging drop vapour diffusion method, using 20% (w/v) PEG 8000, 100 mM magnesium acetate, 100 mM imidazole (pH 6.2), 3% ethylene glycol
-
mutant D154A in complex with MgATP-RNA, hanging drop vapour diffusion method, in 0.1 M bis-Tris propane, pH 6.4, 0.2 M Li-acetate, and 16% PEG 3350; mutant D154A, trapped in complex with ATP and a five residue poly(A). Enzyme has undergone significant domain movement and shows a closed conformation with extensive interactions between substrates and all three polymerase domains
-
tethered to the 3'-end processing complex via Fip1 peptide, hanging drop vapour diffusion method, with 100 mM MES, pH 6.5, 8-10% PEG 20000
-
ATP-gamma-S bound and unbound structures. Subunit VP55 residues of the active site make specific interactions with ATP-gamma-S. Concave surface of subunit VP55 docks the globular subunit VP39. Model of RNA primer binding shows that subunit VP39 functions as a processivity factor by partially enclosing the RNA primer at the heterodimer interface
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
48
-
remains stable at 30C, the melting temperature for the wild type enzyme is at 48C
40
-
-
5 min, stable
45
-
-
5 min, 50% loss of activity
50
-
-
5 min, complete inactivation
50
-
-
reactions incubated at 50C result in a decrease of nearly 50% of incorporation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing and thawing accelerates inactivation
-
the protein undergoes structural modifications upon RNA binding, although the interaction does not significantly modify the stability of the protein
-
a decay of PAP activity with a half-life of approximately 2 h (on ice) is observed when Nonidet-P 40 is omitted from the enzyme storage solution
-
substrates poly(A) and Mg-ATP induce the conformational change, resulting in stabilization of the closed enzyme state and enabling catalysis
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, stable for at least 2 months
-
-20C, 50% glycerol, 80% inactivation in the first few weeks, the 20% remaining activity is stable for more than 2 years
-
-70C or under liquid nitrogen, extensive inactivation
-
-70C, stable
-
-80C, 10-20 mg protein/ml, flash frozen
-
-80C, storage for 5 days including 2 cycles of freezing and thawing results in 35% inactivation
-
-20C, stable for at least 3 months
-
-90C, 50% glycerol, stable for 4 weeks, about 40% loss of activity after 5 months
-
-70C, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
homogenous preparation of bovine enzyme
-
overview: purification methods
-
Ni-NTA agarose column chromatography and phosphocellulose column chromatography
-
overview: purification methods
Coturnix sp., Cricetulus griseus
-
; high salt conditions required during purification
-
HiTrap chelating Sepharose column chromatography
P0ABF1
overview: purification methods
-
The wild-type poly(A) polymerase, as well as deletion variants are expressed in Escherichia coli BL21(DE3) (Novagen). Freshly transformed cells are grown at 28-37C in 700 ml LB medium containing 0.030 mg/ml kanamycin and 0.033 mg/ml chloramphenicol. At mid-log phase (A600 = 0.6), expression is induced by the addition of IPTG to a final concentration of 0.200 mM. After 3-5 hr of incubation at 28-37C, cells are harvested by centrifugation and lysed by lysozyme treatment and sonication in ice-cold buffer I (20 mM Tris/HCl pH 7.6, 0.5 M NaCl, 5 mM imidazole and 0.75 mg/ml lysozyme). After centrifugation for 30 min at 25000 xg and 4C, the proteins in the supernatant are purified by FPLC on a 5 ml HiTrap Chelating Sepharose column (Amersham Biosciences) and eluted with 500 mM imidazole. Fractions containing the enzymes as determined by SDS-PAGE are pooled, dialyzed against buffer II (20 mM Tris/HCl pH 7.6, 0.5 M NaCl, 5 mM MgCl2 and 10% glycerol). All proteins are stored in the presence of 40% (v/v) glycerol at -20C.
-
2 forms from nuclear fraction: NE PAPs I and II, one form from cytoplasmic fraction: S100 PAP
-
by BD TALON Resin (zco, clontechClontech) or nickel-nitrilotriacetic acid-agarose (Qiagen)
-
native tandem affinity column chromatography; Sepharose column chromatography
-
overview: purification methods
-
partial, HeLa cells infected with
-
polymerase IIa and IIb
-
glutathione affinity Sepharose column chromatography
-
overview: purification methods
-
M2 affinity agarose column chromatography
-
adenylyltransferase A and B
-
2 forms, one from chromatin and one from nucleoplasm
-
overview: purification methods
-
Ni-affinity column chromatography
-
nickel affinity column chromatography and ion exchange chromatography
-
polynucleotide adenylyltransferase Trf5p copurifies with Mtr4p and Air1p of the polyadenylation complex
-
recombinant yeast PAP is purified by nickel affinity and anion exchange chromatography using NTA agarose and Source S resins
-
3 forms: Ia, Ib, II
-
overview: purification methods
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli Rosetta (DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Xenopus laevis oocytes
-
expressed in Escherichia coli BL21(DE3) or BL21(DE3)pLys cells
P0ABF1
vector pET30-EK/LIC, expression in Escherichia coli
-
-
Q9BWI3
expressed in 293T cells; expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in COS-1 cells; the full length hmtPAP open reading frame is cloned
-
expression in Escherichia coli
-
expression in HEK-293 cell
Q8NDF8
expression in Xenopus oocyte
-
PAPgamma(1-683C), a C-terminally truncated version of full length human PAPgamma with the same catalytic efficiency is expressed in Escherichia coli
-
expressed in HeLa cells and in Escherichia coli
-
expressed in HeLa cells and NIH 3T3 cells
-
expressed in NIH/3T3 cells
Q9WVP6
expression in Xenopus oocyte
-
expressed in HEK-293 cells
-
expression in Escherichia coli
-
expression in Xenopus oocyte
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C36S/C118V/A152C/C160S/C197S/C257S/C293S/C204V
-
introduction of a Cys residue in a mutant lacking all endogenous Cys residues. Mutant achieves maximum specific disulfide cross-linking efficiency. The resulting construct is active and, when mixed with a chemically modified RNA, yields crystals of an enzyme-RNA complex
C36S/C118V/C160S/C197S/C257S/C293S/C204V
-
mutation of all seven endogenous cysteine residues. Mutant is able to bind RNA at a level similar to that of wild-type, but no longer forms nonspecific disulfide cross-links with the modified RNA
D167N
-
strong reduction of catalytic efficiency
D167N/N202A
-
sharp decrease in catalytic efficiency
D167N/T317G
-
sharp decrease in catalytic efficiency
D167N/V247R
-
sharp decrease in catalytic efficiency
F100D
-
strong reduction of catalytic efficiency
G203H
-
strong reduction of catalytic efficiency
K228A
-
increase in Km for ATP
K232A
-
increase in Km for ATP
N202A
-
high Km value for RNA, strong reduction of catalytic efficiency, incorporates etheno-ATP and N1-methyl-ATP better than wild-type, but incorporates N6-methyl-ATP poorly
N239A
-
kcat for ATP is reduced fourfold
R199A
-
reduces kcat for RNA about 30-fold
T317G
-
increase in Km for ATP, tolerates etheno-ATP and GTP, rejects N6-methyl-ATP
V156A
-
strong reduction of catalytic efficiency
V247R
-
kcat for ATP is reduced 2000-fold, strong reduction of catalytic efficiency
Y237A
-
increase in Km for ATP
D170A
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity
D170P
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity; no detectable AMP incorporation
D212A
P0ABF1
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
D214A
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity
D214P
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity; no detectable AMP incorporation
D79A
-
disparity between Diphosphate release and AMP incorporation
D88A
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity
D88P
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity; no detectable AMP incorporation
D90A
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity
D90P
-
diphosphate release equivalent to AMP production, 5-30% of wild type activity; no detectable AMP incorporation
E211A
P0ABF1
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
G74A
-
disparity between Diphosphate release and AMP incorporation
R215A
P0ABF1
the mutation leads to a dramatic loss in nucleotide specificity and the formation of poly(N) tails
D212A
Escherichia coli K12
-
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
-
E211A
Escherichia coli K12
-
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
-
R215A
Escherichia coli K12
-
the mutation leads to a dramatic loss in nucleotide specificity and the formation of poly(N) tails
-
D325A
-
mutation of one of the conserved Asp residues in the active site, complete loss of activity. The mutant protein gives better quality crystals than the wild-type enzyme
H259A/K260A/I261A
-
mutation in beta-arm, mutant remains dimeric
H259A/K260A/I261A/H294A/F295A/P297A
-
mutations simultaneously disrupt both areas of contact in the dimer interface, mutant is a stable monomer in solution, complete loss of activity
H294A/F295A/P297A
-
mutation in helix alphaE, mutant exists in a monomer-dimer equilibrium
D154A
-
crystallization data, closed conformation with extensive interactions between substrates and all three polymerase domains; the mutant has a nearly identical melting temperature as wild type PAP
K215A
-
74- and 56-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
N189A
-
residue bridges the N and middle domains in the closed state; the mutant has a nearly identical melting temperature as wild type PAP
N226A
-
74- and 56-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme
N226A
-
mutation affects the equilibrium between the open- and closed-domain forms of the enzyme; the mutant has a nearly identical melting temperature as wild type PAP
V498Y/C485R
-
the mutant is unable to bind Fip1 but retains full polymerase activity
Y224F
-
30-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
Y224F
-
altered melting temperature (44C) compared to the wild type enzyme; mutation affects the equilibrium between the open- and closed-domain forms of the enzyme
Y224S
-
12-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
G74P
-
disparity between Diphosphate release and AMP incorporation
additional information
-
chimeras of CCA-adding enzyme and PAP were constructed
additional information
-
enzyme PAP I variant with C-terminal His-tag can be phosphorylated both in vivo and in vitro. In vivo phosphorylation impairs activity of the enzyme
additional information
-
enzyme knockout mutant, the mRNA levels of bolA, which is induced in response to many forms of stress, are reduced 2.5fold in stationary phase. Absence of enzyme enhances the RssB-mediated deltaS proteolysis specifically in starved cells
additional information
-
reengineering of enzyme in order to function as (UG) adding enzyme. Double- and triple-mutants in residues 211, 212, 215 add 570 G residues to oligoA15 substrate
K560E
Q8NDF8
mutation in the C-terminal basic motif. About 20% of wild-type activity
additional information
-
hmtPAP knockdown mutant cells show decreased steady state levels of mtDNA-encoded proteins as well as deficient mitochondrial activities such as oxygen consumption rate
additional information
Q8NDF8
deletion variant of the C-terminal part lacking amino acids 369-551. Whereas the C terminus binds to RNA, the deletion variant shows no shift of the RNA in EMSA experiments
Y221A/F222A
-
mutation in helix alphaB, mutant exists in a monomer-dimer equilibrium
additional information
-
GLD-2 disruption does not affect the poly(A) tail elongation in oocytes
S537A
-
the mutant catalytic domain is not phosphorylated by ERK
additional information
-
the un-17 mutant carries a temperature-sensitive mutation in the gene encoding PAP
K215A
-
2- to 4fold increase in Km values; the mutant has a nearly identical melting temperature as wild type PAP
additional information
-
deletion of C-terminal 31 amino acids has no effect, deletion of C-terminal 67 amino acids affects RNA binding, deletion of N-terminal 18 amino acids eliminates specific activity
additional information
-
mutation of bovine residue N202 (equivalent to yeast N189) to alanine has essentially no effect on the apparent Km for ATP, but has a pronounced effect on the apparent Vmax, suggesting that this residue is particularly important in the recognition of the adenine of ATP
additional information
-
strain lacking the Rrp6p component of the nuclear exosome accumulate polyadenylated forms of different ribosomal RNA precursors. This polyadenylation is reduced in strains lacking polynucleotide adenylyltransferase Trf5p and enhanced in strains overexpressing Trf5p
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
chromatography on MonoQ results in three fractions with little activity, one of them containing a 43000 polypeptide, the others RNAs, mixtures of them result in substantial enzymic activity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
use as prognostic factor for early recurrence and death in breast cancer patients
medicine
Q9BWI3
enzyme is overexpressed in cancers
medicine
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PAP activity is used to measure the effects of anticancer drugs etoposide and cordycepin in two epithelial cancer cell lines, HeLa (human epithelioid cervix carcinoma) and MCF-7 (human breast cancer). MCF-7 is found to express significantly more PAP than the cervical cancer cell line, HeLa. Treatment of HeLa cells with etoposide (0.034 mM) leads to a continuous increase in PAP activity levels during the 2 h of exposure. Important differential modulations in both PAP enzyme activity and isoforms are observed, occurring earlier than chromatin condensation and cleavage, in both epithelial cancer cell lines tested. Treatment of HeLa cells with cordycepin (0.067 mM) leads to a continuous increase in PAP activity and isoform levels after 4 h of exposure. In the case of MCF-7 cells, treatment with 0.067 mM cordycepin leads to a decrease in both PAP II enzyme activity and phosphorylated PAP isoforms after 4 h of exposure. Thus high PAP activity levels in breast cancer cells may be an independent unfavorable prognostic factor contributing to the malignant phenotype of cells. The differentiated modulations of PAP in the two epithelial cancer cell lines correlate to changes in the cell cycle, suggesting that in this case PAP II follows the cell cycle despite the course of apoptosis. Thus in these two epithelial cell lines PAP modulations follow cell cycle progression rather than apoptosis
biotechnology
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assay in microtiter format
drug development
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polyadenylation inhibition represents one mode of action for 8-chloroadenosine and 8-aminoadenosine in hematological malignancies, among several possible mechanisms. RNA-directed drugs may offer a valuable strategy in targeting indolent cancers, such as multiple myeloma