Biochemical Journal, volume 478, issue 7, pages 1399-1412

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

Shilkin Evgeniy S. ¹

Gromova Anastasia S. ¹

Smal Margarita P. ²

Макарова А. В. ¹

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Institute of Molecular Genetics, National Research Center «Kurchatov Institute», Kurchatov sq. 2, 123182 Moscow, Russia

Institute of Molecular Genetics of NRC «Kurchatov Institute»

National Research Centre "Kurchatov Institute"

Institute of Genetics and Cytology of the National Academy of Sciences of Belarus, 220072 Minsk, Republic of Belarus |

Publication type: Journal Article

Publication date: 2021-02-19

Portland Press

Journal: Biochemical Journal

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Impact factor: 4.1

ISSN: 02646021, 14708728, 03063283, 00062936

DOI: 10.1042/bcj20200491

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Biochemistry

Molecular Biology

Cell Biology

Abstract

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.

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International Journal of Biological Macromolecules	International Journal of Biological Macromolecules, 1, 100% International Journal of Biological Macromolecules 1 publication, 100%
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Shilkin E. S. et al. DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol ι // Biochemical Journal. 2021. Vol. 478. No. 7. pp. 1399-1412.

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Shilkin E. S., Gromova A. S., Smal M. P., Макарова А. В. DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol ι // Biochemical Journal. 2021. Vol. 478. No. 7. pp. 1399-1412.

RIS |

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TY - JOUR

DO - 10.1042/bcj20200491

UR - https://doi.org/10.1042%2Fbcj20200491

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

T2 - Biochemical Journal

AU - Shilkin, Evgeniy S.

AU - Gromova, Anastasia S.

AU - Smal, Margarita P.

AU - Макарова, А. В.

PY - 2021

DA - 2021/02/19 00:00:00

PB - Portland Press

SP - 1399-1412

IS - 7

VL - 478

SN - 0264-6021

SN - 1470-8728

SN - 0306-3283

SN - 0006-2936

ER -

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@article{2021_Shilkin,

author = {Evgeniy S. Shilkin and Anastasia S. Gromova and Margarita P. Smal and А. В. Макарова},

title = {DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol ι},

journal = {Biochemical Journal},

year = {2021},

volume = {478},

publisher = {Portland Press},

month = {feb},

url = {https://doi.org/10.1042%2Fbcj20200491},

number = {7},

pages = {1399--1412},

doi = {10.1042/bcj20200491}

}

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Shilkin, Evgeniy S., et al. “DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol ι.” Biochemical Journal, vol. 478, no. 7, Feb. 2021, pp. 1399-1412. https://doi.org/10.1042%2Fbcj20200491.

Found error?

Publisher

Portland Press

Journal

Biochemical Journal

Quartile SCImago

Quartile WOS

Impact factor

4.1

ISSN

02646021 (Print)
14708728 (Electronic)
03063283 (Print)
00062936 (Print)

Labs

Laboratory of mechanisms of replication of damaged DNA

Profiles

Makarova, Alena Vladimirovna