期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:2001
卷号:98
期号:15
页码:8350-8354
DOI:10.1073/pnas.111007198
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:DNA polymerase V, composed of a heterotrimer of the DNA damage-inducible UmuC and UmuD[IMG]f1.gif" ALT="Formula" BORDER="0"> proteins, working in conjunction with RecA, single-stranded DNA (ssDNA)-binding protein (SSB), {beta} sliding clamp, and {gamma} clamp loading complex, are responsible for most SOS lesion-targeted mutations in Escherichia coli, by catalyzing translesion synthesis (TLS). DNA polymerase II, the product of the damage-inducible polB (dinA ) gene plays a pivotal role in replication-restart, a process that bypasses DNA damage in an error-free manner. Replication-restart takes place almost immediately after the DNA is damaged ({approx}2 min post-UV irradiation), whereas TLS occurs after pol V is induced {approx}50 min later. We discuss recent data for pol V-catalyzed TLS and pol II-catalyzed replication-restart. Specific roles during TLS for pol V and each of its accessory factors have been recently determined. Although the precise molecular mechanism of pol II-dependent replication-restart remains to be elucidated, it has recently been shown to operate in conjunction with RecFOR and PriA proteins.