Journal
MOLECULAR CELL
Volume 35, Issue 1, Pages 105-115Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2009.05.026
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Funding
- NCI NIH HHS [P01 CA092584, P01CA092584] Funding Source: Medline
- NIGMS NIH HHS [R01 GM052504-12A1, R01 GM045948-17A1, R01 GM045948-18, R01 GM045948, GM045948, R01 GM059902, R01 GM052504] Funding Source: Medline
- WETP NIH HHS [WT076476] Funding Source: Medline
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Rad51 is a DNA recombinase functioning in the repair of DNA double-strand breaks and the generation of genetic diversity by homologous recombination (HR). In the presence of ATP, Rad51 self-assembles into an extended polymer on single-stranded DNA to catalyze strand exchange. Inappropriate HR causes genomic instability, and it is normally prevented by remodeling enzymes that antagonize the activities of Rad51 nucleoprotein filaments. In yeast, the Srs2 helicase/translocase suppresses HR by clearing Rad51 polymers from single-stranded DNA. We have examined the mechanism of disassembly of Rad51 nucleoprotein filaments by Srs2 and find that a physical interaction between Rad51 and the C-terminal region of Srs2 triggers ATP hydrolysis within the Rad51 filament, causing Rad51 to dissociate from DNA. This allosteric mechanism explains the biological specialization of Srs2 as a DNA motor protein that antagonizes HR.
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