Rad54 protein is targeted to pairing loci by the Rad51 nucleoprotein filament

被引：156
作者：
Mazin, AV
Bornarth, CJ
Solinger, JA
Heyer, WD
Kowalczykowski, SC [1 ]
机构：
[1] Univ Calif Davis, Div Biol Sci, Microbiol Sect, Davis, CA 95616 USA
[2] Univ Calif Davis, Sect Mol & Cellular Biol, Davis, CA 95616 USA
来源：
MOLECULAR CELL | 2000年 / 6卷 / 03期
关键词：
D O I：
10.1016/S1097-2765(00)00057-5
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：
Rad51 and Rad54 proteins are important for the repair of double-stranded DNA (dsDNA) breaks by homologous recombination in eukaryotes. Rad51 assembles on single-stranded DNA (ssDNA) to form a helical nucleoprotein filament that performs homologous pairing with dsDNA; Rad54 stimulates this pairing substantially. Here, we demonstrate that Rad54 acts in concert with the mature Rad51-ssDNA filament. Enhancement of DNA pairing by Rad54 is greatest at an equimolar ratio relative to Rad51 within the filament. Reciprocally, the Rad51-ssDNA filament enhances both the dsDNA-dependent ATPase and the dsDNA unwinding activities of Rad54. We conclude that Rad54 participates in the DNA homology search as a component of the Rad51-nucleoprotein filament and that the filament delivers Rad54 to the dsDNA pairing locus, thereby linking the unwinding of potential target DNA with the homology search process.
引用
收藏
页码：583 / 592
页数：10
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