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Rad51 Paralogs Remodel Pre-synaptic Rad51 Filaments to Stimulate Homologous Recombination
MR. Taylor, M. Špírek, KR. Chaurasiya, JD. Ward, R. Carzaniga, X. Yu, EH. Egelman, LM. Collinson, D. Rueda, L. Krejci, SJ. Boulton,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Cell Press Free Archives
from 1995-01-01 to 1 year ago
Free Medical Journals
from 1995 to 1 year ago
Open Access Digital Library
from 1995-01-01
Elsevier Open Access Journals
from 1995-01-13 to 2023-06-22
Elsevier Open Archive Journals
from 1995-01-13 to 1 year ago
- MeSH
- Caenorhabditis elegans metabolism MeSH
- DNA-Binding Proteins genetics metabolism MeSH
- HEK293 Cells MeSH
- Homologous Recombination * MeSH
- DNA, Single-Stranded metabolism MeSH
- Nuclear Pore Complex Proteins metabolism MeSH
- Humans MeSH
- Mutation MeSH
- Caenorhabditis elegans Proteins genetics metabolism MeSH
- Rad51 Recombinase metabolism MeSH
- Saccharomyces cerevisiae Proteins metabolism MeSH
- Saccharomyces cerevisiae metabolism MeSH
- Carrier Proteins metabolism MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Repair of DNA double strand breaks by homologous recombination (HR) is initiated by Rad51 filament nucleation on single-stranded DNA (ssDNA), which catalyzes strand exchange with homologous duplex DNA. BRCA2 and the Rad51 paralogs are tumor suppressors and critical mediators of Rad51. To gain insight into Rad51 paralog function, we investigated a heterodimeric Rad51 paralog complex, RFS-1/RIP-1, and uncovered the molecular basis by which Rad51 paralogs promote HR. Unlike BRCA2, which nucleates RAD-51-ssDNA filaments, RFS-1/RIP-1 binds and remodels pre-synaptic filaments to a stabilized, "open," and flexible conformation, in which the ssDNA is more accessible to nuclease digestion and RAD-51 dissociation rate is reduced. Walker box mutations in RFS-1, which abolish filament remodeling, fail to stimulate RAD-51 strand exchange activity, demonstrating that remodeling is essential for RFS-1/RIP-1 function. We propose that Rad51 paralogs stimulate HR by remodeling the Rad51 filament, priming it for strand exchange with the template duplex.
Department of Biology Masaryk University 62500 Brno Czech Republic
National Centre for Biomolecular Research Masaryk University 62500 Brno Czech Republic
UCSF Mission Bay Genentech Hall S574 San Francisco CA 94158 USA
References provided by Crossref.org
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- $a Repair of DNA double strand breaks by homologous recombination (HR) is initiated by Rad51 filament nucleation on single-stranded DNA (ssDNA), which catalyzes strand exchange with homologous duplex DNA. BRCA2 and the Rad51 paralogs are tumor suppressors and critical mediators of Rad51. To gain insight into Rad51 paralog function, we investigated a heterodimeric Rad51 paralog complex, RFS-1/RIP-1, and uncovered the molecular basis by which Rad51 paralogs promote HR. Unlike BRCA2, which nucleates RAD-51-ssDNA filaments, RFS-1/RIP-1 binds and remodels pre-synaptic filaments to a stabilized, "open," and flexible conformation, in which the ssDNA is more accessible to nuclease digestion and RAD-51 dissociation rate is reduced. Walker box mutations in RFS-1, which abolish filament remodeling, fail to stimulate RAD-51 strand exchange activity, demonstrating that remodeling is essential for RFS-1/RIP-1 function. We propose that Rad51 paralogs stimulate HR by remodeling the Rad51 filament, priming it for strand exchange with the template duplex.
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