NON-CATALYTIC DOMAINS OF DNA POLYMERASE λ: INFLUENCE ON ENZYME ACTIVITY AND ITS REGULATION

Ekaterina A. Maltseva; Мальцева Е. А.; Nadejda I. Rechkunova; Речкунова Н. И.; Olga. I. Lavrik; Лаврик О. И.

doi:10.31857/S2686738923600358

NON-CATALYTIC DOMAINS OF DNA POLYMERASE λ: INFLUENCE ON ENZYME ACTIVITY AND ITS REGULATION

Authors: Maltseva E.A.¹, Rechkunova N.I.¹, Lavrik O.I.¹
Affiliations:
1. Institute of Chemical Biology and Fundamental Medicine Siberian Branch of Russian Academy of Sciences
Issue: Vol 512, No 1 (2023)
Pages: 422-427
Section: Articles
URL: https://vestnik.nvsu.ru/2686-7389/article/view/651066
DOI: https://doi.org/10.31857/S2686738923600358
EDN: https://elibrary.ru/OZLFUZ
ID: 651066

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Abstract
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Abstract

DNA polymerase λ (Polλ) belongs to the same structural X-family as DNA polymerase β, the main polymerase of base excision repair. The role of Polλ in this process remains not fully understood. A significant difference between the two DNA polymerases is the presence of an extended non-catalytic N-terminal region in the Polλ structure. The influence of this region on the interaction of Polλ with DNA and multifunctional proteins, poly(ADP-ribose)polymerase 1 (PARP1) and replication protein A (RPA), was studied in detail for the first time. The data obtained suggest that non-catalytic Polλ domains play a suppressor role both in relation to the polymerase activity of the enzyme and in interaction with DNA and PARP1.

Keywords

base excision repair, DNA polymerases, PARP1, activity regulation

References

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