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

Авторлар: Maltseva E.¹, Rechkunova N.¹, Lavrik O.¹
Мекемелер:
1. Institute of Chemical Biology and Fundamental Medicine Siberian Branch of Russian Academy of Sciences
Шығарылым: Том 512, № 1 (2023)
Беттер: 422-427
Бөлім: Articles
URL: https://journals.rcsi.science/2686-7389/article/view/140837
DOI: https://doi.org/10.31857/S2686738923600358
EDN: https://elibrary.ru/OZLFUZ
ID: 140837

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Аннотация
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Әдебиет тізімі
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Статистика

Аннотация

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.

Негізгі сөздер

base excision repair, DNA polymerases, PARP1, activity regulation

Әдебиет тізімі

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