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Human replication protein A - The C-terminal RPA70 and the central RPA32 domains are involved in the interactions with the 3 '-end of a primer-template DNAстатья Исследовательская статья
Статья опубликована в высокорейтинговом журнале
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: 17 апреля 2018 г.
- Авторы: Pestryakov P.E., Weisshart K., Schlott B., Khodyreva S.N., Kremmer E., Grosse F., Lavrik O.I., Nasheuer H.P.
- Журнал: Journal of Biological Chemistry
- Том: 278
- Номер: 19
- Год издания: 2003
- Издательство: American Society for Biochemistry and Molecular Biology Inc.
- Местоположение издательства: United States
- Первая страница: 17515
- Последняя страница: 17524
- DOI: 10.1074/jbc.M301265200
- Аннотация: Although the mechanical aspects of the single-stranded DNA (ssDNA) binding activity of human replication protein A (RPA) have been extensively studied, only limited information is available about its interaction with other physiologically relevant DNA structures. RPA interacts with partial DNA duplexes that resemble DNA intermediates found in the processes of DNA replication and DNA repair. Limited proteolysis of RPA showed that RPA associated with ssDNA is less protected against proteases than RPA bound to a partial duplex DNA containing a 5'-protruding tail that had the same length as the ssDNA. Modification of both the 70- and 32-kDa subunits, RPA70 and RPA32, respectively, by photoaffinity labeling indicates that RPA can bind the primer-template junction of partial duplex DNAs by interacting with the 3'-end of the primer. The identification of the protein domains modified by the photoreactive 3'-end of the primer showed that domains located in the central part of the RPA32 subunit (amino acids 39 180) and the C-terminal part of the RPA70 subunit (amino acids 432-616) are involved in these interactions.
- Добавил в систему: Пестряков Павел Ефимович