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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Antony E,Tomko EJ,Xiao Q,Krejci L,Lohman TM,Ellenberger Tdoi
10.1016/j.molcel.2009.05.026subject
Has Abstractpub_date
2009-07-10 00:00:00pages
105-15issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(09)00387-6journal_volume
35pub_type
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