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Effect of the multifunctional proteins RPA, YB-1, and XPC repair factor on AP site cleavage by DNA glycosylase NEIL1статья Исследовательская статья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 10 апреля 2018 г.
- Авторы: Pestryakov Pavel, Zharkov Dmitry O., Grin Inga, Fomina Elizaveta E., Kim Ekaterina R., Hamon Loic, Eliseeva Irina A., Petruseva Irina O., Curmi Patrick A., Ovchinnikov Lev P., Lavrik Olga I.
- Журнал: Journal of Molecular Recognition
- Том: 25
- Номер: 4
- Год издания: 2012
- Издательство: John Wiley & Sons Inc.
- Местоположение издательства: United States
- Первая страница: 224
- Последняя страница: 233
- DOI: 10.1002/jmr.2182
- Аннотация: DNA glycosylases are key enzymes in the first step of base excision DNA repair, recognizing DNA damage and catalyzing the release of damaged nucleobases. Bifunctional DNA glycosylases also possess associated apurinic/apyrimidinic (AP) lyase activity that nick the damaged DNA strand at an abasic (or AP) site, formed either spontaneously or at the first step of repair. NEIL1 is a bifunctional DNA glycosylase capable of processing lesions, including AP sites, not only in double-stranded but also in single-stranded DNA. Here, we show that proteins participating in DNA damage response, YB-1 and RPA, affect AP site cleavage by NEIL1. Stimulation of the AP lyase activity of NEIL1 was observed when an AP site was located in a 60?nt-long double-stranded DNA. Both RPA and YB-1 inhibited AP site cleavage by NEIL1 when the AP site was located in single-stranded DNA. Taking into account a direct interaction of YB-1 with the AP site, located in single-stranded DNA, and the high affinity of both YB-1 and RPA for single-stranded DNA, this behavior is presumably a consequence of a competition with NEIL1 for the DNA substrate. Xeroderma pigmentosum complementation group C protein (XPC), a key protein of another DNA repair pathway, was shown to interact directly with AP sites but had no effect on AP site cleavage by NEIL1. Copyright (c) 2012 John Wiley & Sons, Ltd.
- Добавил в систему: Пестряков Павел Ефимович