Document Detail


Dynamic regulatory interactions of rad51, rad52, and replication protein-a in recombination intermediates.
MedLine Citation:
PMID:  19445949     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Rad51, Rad52, and replication protein-A (RPA) play crucial roles in the repair of DNA double-strand breaks in Saccharomyces cerevisiae. Rad51 mediates DNA strand exchange, a key reaction in DNA recombination. Rad52 recruits Rad51 into single-stranded DNAs (ssDNAs) that are saturated with RPA. Rad52 also promotes annealing of ssDNA strands that are complexed with RPA. Specific protein-protein interactions are involved in these reactions. Here we report new biochemical characteristics of these protein interactions. First, Rad52-RPA interaction requires multiple molecules of RPA to be associated with ssDNA, suggesting that multiple contacts between the Rad52 ring and RPA-ssDNA filament are needed for stable binding. Second, RPA-t11, which is a recombination-deficient mutant of RPA, displays a defect in interacting with Rad52 in the presence of salt above 50 mM, explaining the defect in Rad52-mediated ssDNA annealing in the presence of this mutation. Third, ssDNA annealing promoted by Rad52 is preceded by aggregation of multiple RPA-ssDNA complexes with Rad52, and Rad51 inhibits this aggregation. These results suggest a regulatory role for Rad51 that suppresses ssDNA annealing and facilitates DNA strand invasion. Finally, the Rad51-double-stranded DNA complex disrupts Rad52-RPA interaction in ssDNA and titrates Rad52 from RPA. This suggests an additional regulatory role for Rad51 following DNA strand invasion, where Rad51-double-stranded DNA may inhibit illegitimate second-end capture to ensure the error-free repair of a DNA double-strand break.
Authors:
Tomohiko Sugiyama; Noriko Kantake
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-05-13
Journal Detail:
Title:  Journal of molecular biology     Volume:  390     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2009 Jul 
Date Detail:
Created Date:  2009-06-15     Completed Date:  2009-07-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  45-55     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Ohio University, Athens, 45701, USA. sugiyama@ohio.edu
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MeSH Terms
Descriptor/Qualifier:
DNA / metabolism
DNA Repair*
DNA, Single-Stranded / metabolism
Models, Biological
Protein Binding
Protein Interaction Mapping*
Rad51 Recombinase / metabolism*
Rad52 DNA Repair and Recombination Protein / metabolism*
Recombination, Genetic*
Replication Protein A / metabolism*
Saccharomyces cerevisiae / physiology*
Saccharomyces cerevisiae Proteins / metabolism*
Chemical
Reg. No./Substance:
0/DNA, Single-Stranded; 0/RAD52 protein, S cerevisiae; 0/Rad52 DNA Repair and Recombination Protein; 0/Replication Protein A; 0/Saccharomyces cerevisiae Proteins; 9007-49-2/DNA; EC 2.7.7.-/RAD51 protein, S cerevisiae; EC 2.7.7.-/Rad51 Recombinase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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