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.
Recommended Citation
Antony, Edwin; Tomko, Eric J.; Xiao, Qi; Krejci, Lumir; Lohman, Timothy M.; and Ellenberger, Tom, "Srs2 Disassembles Rad51 Filaments by a Protein-Protein Interaction Triggering ATP Turnover and Dissociation of Rad51 from DNA" (2009). Biological Sciences Faculty Research and Publications. 416.
https://epublications.marquette.edu/bio_fac/416
Comments
Accepted version. Molecular Cell, Vol. 35, No. 1 (July 2009): 105-115. DOI. © 2009 Elsevier (Cell Press). Used with permission.
Edwin Antony was affiliated with Washington University at time of publication.