Terminal association of Rad54 protein with the Rad51-dsDNA filament

被引:52
作者
Kiianitsa, Konstantin
Solinger, Jachen A.
Heyer, Wolf-Dietrich [1 ]
机构
[1] Univ Calif Davis, Microbiol Sect, Davis, CA 95616 USA
[2] Univ Calif Davis, Sect Mol & Cellular Biol, Ctr Genet & Dev, Davis, CA 95616 USA
关键词
recombination; ATPase; Snf2-like proteins;
D O I
10.1073/pnas.0604240103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Rad54 protein is a Snf2-related dsDNA-specific ATPase essential for homologous recombination mediated by Rad51 protein, the eukaryotic RecA ortholog. Snf2-related enzymes couple ATP hydrolysis with translocation on dsDNA to remodel or dissociate a wide variety of protein-dsDNA complexes. Rad54 and Rad51 interact through species-specific contacts and mutually stimulate their biochemical activities. Specifically, Rad51 bound to dsDNA, the product of homologous recombination after DNA-strand exchange, stimulates the Rad54 ATPase up to 6-fold, leading to the turnover of Rad51 in the product complex. Electron microscopy visualized the Rad51-Rad54 interaction on dsDNA, showing that an oligomeric form of Rad54 associates preferentially with termini of the Rad51-dsDNA filament. Our data support a mechanism of processive dsDNA-Rad51 filament dissociation by the translocating Rad54 protein.
引用
收藏
页码:9767 / 9772
页数:6
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