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0.0197
2-aminopurine riboside triphosphate
-
0.0005 - 0.037
oligo(A)14
-
0.0263
oligo(A)17C
-
incubation at 30 °C for 15 min in the presence of MgATP2-
-
0.0468 - 0.0642
oligo(A)18
-
additional information
additional information
-
dependence on divalent cation concentration
-
0.0468
(A)n
wild-type, pH 7.0, 30°C
0.106
(A)n
mutant N189A, pH 7.0, 30°C
0.195
(A)n
mutant K215A, pH 7.0, 30°C
0.367
(A)n
mutant N226A, pH 7.0, 30°C
0.711
(A)n
mutant Y224F, pH 7.0, 30°C
0.0359
ATP
-
0.036
ATP
wild-type, pH 7.0, 30°C
0.08
ATP
mutant N189A, pH 7.0, 30°C
0.249
ATP
mutant N226A, pH 7.0, 30°C
0.406
ATP
mutant K215A, pH 7.0, 30°C
0.929
ATP
mutant Y224F, pH 7.0, 30°C
0.104
CTP
wild-type, pH 7.0, 30°C
0.14
CTP
mutant N226A, pH 7.0, 30°C
0.148
CTP
mutant N189A, pH 7.0, 30°C
0.368
CTP
mutant K215A, pH 7.0, 30°C
4.7
CTP
mutant Y224F, pH 7.0, 30°C
0.055
GTP
mutant N226A, pH 7.0, 30°C
0.062
GTP
wild-type, pH 7.0, 30°C
0.031
ATP
-
mutant Y224S
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)
0.0005
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
-
0.0468
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-
-
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V498Y/C485R
the mutant is unable to bind Fip1 but retains full polymerase activity
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
N226A
-
74- and 56-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme
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
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
D154A
crystallization data, closed conformation with extensive interactions between substrates and all three polymerase domains
D154A
the mutant has a nearly identical melting temperature as wild type PAP
K215A
2- to 4fold increase in Km values
K215A
the mutant has a nearly identical melting temperature as wild type PAP
N189A
residue bridges the N and middle domains in the closed state
N189A
the mutant has a nearly identical melting temperature as wild type PAP
N226A
mutation affects the equilibrium between the open- and closed-domain forms of the enzyme
N226A
the mutant has a nearly identical melting temperature as wild type PAP
Y224F
mutation affects the equilibrium between the open- and closed-domain forms of the enzyme
Y224F
altered melting temperature (44°C) compared to the wild type enzyme
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
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Saccharomyces cerevisiae
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Kinetic studies of yeast polyA polymerase indicate an induced fit mechanism for nucleotide specificity
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44
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Saccharomyces cerevisiae
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279
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Saccharomyces cerevisiae
brenda
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Mutations in the middle domain of yeast poly(A) polymerase affect interactions with RNA but not ATP
RNA
10
558-564
2004
Saccharomyces cerevisiae
brenda
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Yeast Trf5p is a nuclear poly(A) polymerase
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7
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2006
Saccharomyces cerevisiae
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Mechanism of poly(A) polymerase: Structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis
Structure
15
1117-1131
2007
Saccharomyces cerevisiae (P29468), Saccharomyces cerevisiae
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Meinke, G.; Ezeokonkwo, C.; Balbo, P.; Stafford, W.; Moore, C.; Bohm, A.
Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein
Biochemistry
47
6859-6869
2008
Saccharomyces cerevisiae (P29468), Saccharomyces cerevisiae
brenda
Balbo, P.B.; Toth, J.; Bohm, A.
X-ray crystallographic and steady state fluorescence characterization of the protein dynamics of yeast polyadenylate polymerase
J. Mol. Biol.
366
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2007
Saccharomyces cerevisiae (P29468), Saccharomyces cerevisiae
brenda
Mellman, D.L.; Gonzales, M.L.; Song, C.; Barlow, C.A.; Wang, P.; Kendziorski, C.; Anderson, R.A.
A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs
Nature
451
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2008
Saccharomyces cerevisiae
brenda
Holbein, S.; Freimoser, F.M.; Werner, T.P.; Wengi, A.; Dichtl, B.
Cordycepin-hypersensitive growth links elevated polyphosphate levels to inhibition of poly(A) polymerase in Saccharomyces cerevisiae
Nucleic Acids Res.
36
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2008
Bos taurus, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Ezeokonkwo, C.; Ghazy, M.A.; Zhelkovsky, A.; Yeh, P.C.; Moore, C.
Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae
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586
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2012
Saccharomyces cerevisiae (P29468), Saccharomyces cerevisiae
brenda
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Interaction between the RNA-dependent ATPase and poly(A) polymerase subunits of the TRAMP complex is mediated by short peptides and important for snoRNA processing
Nucleic Acids Res.
43
1848-1858
2015
Saccharomyces cerevisiae (P48561)
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