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Interaction of nucleotide excision repair factors XPC-HR23B, XPA and RPA with damaged DNAстатья
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: 18 июля 2013 г.
- Авторы: Krasikova Yu S., Rechkunova N.I., Maltseva E.A., Petruseva I.O., Silnikov V.N., Zatsepin T.S., Oretskaya T.S., Sherer O.D., Lavrik O.I.
- Журнал: Biochemistry (Moscow)
- Том: 73
- Номер: 8
- Год издания: 2008
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 886
- Последняя страница: 896
- DOI: 10.1134/S0006297908080063
- Аннотация: The interaction of nucleotide excision repair factors, Xeroderma pigmentosum complementation group C protein in complex with human homolog of RAD23B (XPC-HR23B), replication protein A (RPA), and Xeroderma pigmentosum complementation group A factor (XPA) with 48-mer DNA duplexes imitating damaged DNA structures were investigated. It is demonstrated that the studied proteins exhibit low specificity of binding to damaged DNA compared to undamaged DNA-duplexes. RPA stimulates XPC-HR23B-DNA complex formation, and when XPA and XPC-HR23B are added simultaneously to DNA, a synergistic effect in binding of these proteins with DNA is observed. RPA cross-links to DNA containing photoreactive nucleotide residue, 5I-dUMP, in one of the strands and fluorescein substituted analogs of dUMP as a bulky lesion in the opposite strand of DNA-duplex and stimulates cross-linking of XPC-HR23B. Therefore, RPA may be one of the main regulation factors at different stages of the nucleotide excision repair process. The data are in agreement with the model of the random order assembly that proposes cooperative damage recognition by NER factors forming preincision complex.
- Добавил в систему: Зацепин Тимофей Сергеевич