Modulation of RecA nucleoprotein function by the mutagenic UmuD′C protein complex

被引:34
作者
Rehrauer, WM
Bruck, I
Woodgate, R
Goodmann, MF
Kowalczykowski, SC
机构
[1] Univ Calif Davis, Microbiol Sect, Div Biol Sci, Davis, CA 95616 USA
[2] Univ Calif Davis, Sect Mol & Cellular Biol, Div Biol Sci, Davis, CA 95616 USA
[3] Univ So Calif, Dept Biol Sci, Hedco Mol Biol Labs, Los Angeles, CA 90089 USA
[4] NICHD, Sect DNA Replicat Repair & Mutagenesis, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1074/jbc.273.49.32384
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The RecA, UmuC, and UmuD' proteins are essential for error-prone, replicative bypass of DNA lesions. Normally, RecA protein mediates homologous pairing of DNA. We show that purified Umu(D')(2)C blocks this recombination function. Biosensor measurements establish that the mutagenic complex binds to the RecA nucleoprotein filament with a stoichiometry of one Umu(D')(2)C complex for every two RecA monomers, Furthermore, Umu(D')(2)C competitively inhibits LexA repressor cleavage but not ATPase activity, implying that Umu(D')(2)C binds in or proximal to the helical groove of the RecA nucleoprotein filament. This binding reduces joint molecule formation and even more severely impedes DNA heteroduplex formation by RecA protein, ultimately blocking all DNA pairing activity and thereby abridging participation in recombination function. Thus, Umu(D')(2)C restricts the activities of the RecA nucleoprotein filament and presumably, in this manner, recruits it for mutagenic repair function. This modulation by Umu(D')(2)C is envisioned as a key event in the transition from a normal mode of genomic maintenance by "error-free" recombinational repair, to one of "error-prone" DNA replication.
引用
收藏
页码:32384 / 32387
页数:4
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