Document Type

Article

Language

eng

Format of Original

11 p.

Publication Date

7-2009

Publisher

Elsevier

Source Publication

Molecular Cell

Source ISSN

1097-2765

Original Item ID

DOI: 10.1016/j.molcel.2009.05.026

Abstract

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.

Comments

Accepted version. Molecular Cell, Vol. 35, No. 1 (July 2009): 105-115. DOI. © Elsevier (Cell Press) 2009. Used with permission.

Edwin Antony was affiliated with Washington University at time of publication.

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