scholarly journals DNA Polymerase Iota

2020 ◽  
Author(s):  
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Iota

scholarly journals DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol ι

2021 ◽  
Vol 478 (7) ◽  
pp. 1399-1412
Author(s):  
Evgeniy S. Shilkin ◽  
Anastasia S. Gromova ◽  
Margarita P. Smal ◽  
Alena V. Makarova
Keyword(s):  
Dna Damage ◽  
Dna Polymerase ◽  
Polymerase Activity ◽  
Altered Expression ◽  
Dna Polymerase Iota ◽  
Nucleotide Incorporation ◽  
Lyase Activity ◽  
Polymorphic Variants ◽  
Y Family

Y-family DNA polymerase iota (Pol ι) is involved in DNA damage response and tolerance. Mutations and altered expression level of POLI gene are linked to a higher incidence of cancer. We biochemically characterized five active site polymorphic variants of human Pol ι: R71G (rs3218778), P118L (rs554252419), I236M (rs3218784), E251K (rs3218783) and P365R (rs200852409). We analyzed fidelity of nucleotide incorporation on undamaged DNA, efficiency and accuracy of DNA damage bypass, as well as 5′-deoxyribophosphate lyase (dRP-lyase) activity. The I236M and P118L variants were indistinguishable from the wild-type Pol ι in activity. The E251K and P365R substitutions altered the spectrum of nucleotide incorporation opposite several undamaged DNA bases. The P365R variant also reduced the dRP-lyase activity and possessed the decreased TLS activity opposite 8-oxo-G. The R71G mutation dramatically affected the catalytic activities of Pol ι. The reduced DNA polymerase activity of the R71G variant correlated with an enhanced fidelity of nucleotide incorporation on undamaged DNA, altered lesion-bypass activity and reduced dRP-lyase activity. Therefore, this amino acid substitution likely alters Pol ι functions in vivo.

scholarly journals Inaccurate DNA Synthesis in Cell Extracts of Yeast Producing Active Human DNA Polymerase Iota

PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e16612 ◽  
Author(s):  
Alena V. Makarova ◽  
Corinn Grabow ◽  
Leonid V. Gening ◽  
Vyacheslav Z. Tarantul ◽  
Tahir H. Tahirov ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Dna Polymerase Iota ◽  
Cell Extracts ◽  
Human Dna

Roles of the active site residues and metal cofactors in noncanonical base-pairing during catalysis by human DNA polymerase iota

DNA Repair ◽  
2014 ◽  
Vol 22 ◽  
pp. 67-76 ◽  
Author(s):  
Alena V. Makarova ◽  
Artem Ignatov ◽  
Nataliya Miropolskaya ◽  
Andrey Kulbachinskiy
Keyword(s):  
Dna Polymerase ◽  
Active Site ◽  
Active Site Residues ◽  
Base Pairing ◽  
Dna Polymerase Iota ◽  
Human Dna ◽  
Metal Cofactors

A false note of DNA polymerase iota in the choir of genome caretakers in mammals

2006 ◽  
Vol 71 (2) ◽  
pp. 155-159 ◽  
Author(s):  
L. V. Gening ◽  
A. V. Makarova ◽  
A. M. Malashenko ◽  
V. Z. Tarantul
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Iota

Effect of Mn(II) on error-prone DNA polymerase iota activity in extracts from human normal and tumor cells

2013 ◽  
Vol 28 (1) ◽  
pp. 1-7 ◽  
Author(s):  
A. V. Lakhin ◽  
A. S. Efremova ◽  
I. V. Makarova ◽  
E. E. Grishina ◽  
S. I. Shram ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Dna Polymerase ◽  
Dna Polymerase Iota

scholarly journals DNA polymerase iota and related Rad30–like enzymes

2001 ◽  
Vol 356 (1405) ◽  
pp. 53-60 ◽  
Author(s):  
John P. McDonald ◽  
Agnès Tissier ◽  
Ekaterina G. Frank ◽  
Shigenori Iwai ◽  
Fumio Hanaoka ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Xeroderma Pigmentosum ◽  
Molecular Mechanisms ◽  
Dna Polymerases ◽  
Cellular Functions ◽  
Translesion Dna Synthesis ◽  
Dna Polymerase Iota ◽  
Biochemical Studies ◽  
Template Dna

Until recently, the molecular mechanisms of translesion DNA synthesis (TLS), a process whereby a damaged base is used as a template for continued replication, was poorly understood. This area of scientific research has, however, been revolutionized by the finding that proteins long implicated in TLS are, in fact, DNA polymerases. Members of this so–called UmuC/DinB/Rev1/Rad30 superfamily of polymerases have been identified in prokaryotes, eukaryotes and archaea. Biochemical studies with the highly purified polymerases reveal that some, but not all, can traverse blocking lesions in template DNA. All of them share a common feature, however, in that they exhibit low fidelity when replicating undamaged DNA. Of particular interest to us is the Rad30 subfamily of polymerases found exclusively in eukaryotes. Humans possess two Rad30 paralogs, Rad30A and Rad30B. The RAD30A gene encodes DNA polymerase η and defects in the protein lead to the xeroderma pigmentosum variant (XP–V) phenotype in humans. Very recently RAD30B has also been shown to encode a novel DNA polymerase, designated as Pol ι. Based upon in vitro studies, it appears that Pol ι has the lowest fidelity of any eukaryotic polymerase studied to date and we speculate as to the possible cellular functions of such a remarkably error–prone DNA polymerase.

Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota

Nature ◽  
2002 ◽  
Vol 419 (6910) ◽  
pp. 944-947 ◽  
Author(s):  
Ahmad Faili ◽  
Said Aoufouchi ◽  
Eric Flatter ◽  
Quentin Guéranger ◽  
Claude-Agnès Reynaud ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Somatic Hypermutation ◽  
Immunoglobulin Genes ◽  
Dna Polymerase Iota
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