GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

PMID:9679065

From GONUTS
Jump to: navigation, search
Citation

Gasior, SL, Wong, AK, Kora, Y, Shinohara, A and Bishop, DK (1998) Rad52 associates with RPA and functions with rad55 and rad57 to assemble meiotic recombination complexes. Genes Dev. 12:2208-21

Abstract

We show that the Saccharomyces cerevisiae recombination protein Rad52 and the single-strand DNA-binding protein RPA assemble into cytologically detectable subnuclear complexes (foci) during meiotic recombination. Immunostaining shows extensive colocalization of Rad52 and RPA and more limited colocalization of Rad52 with the strand exchange protein Rad51. Rad52 and RPA foci are distinct from those formed by Rad51, and its meiosis-specific relative Dmc1, in that they are also detected in meiosis during replication. In addition, RPA foci are observed during mitotic S phase. Double-strand breaks (DSBs) promote formation of RPA, Rad52, and Rad51 foci. Mutants that lack Spo11, a protein required for DSB formation, are defective in focus formation, and this defect is suppressed by ionizing radiation in a dose-dependent manner. DSBs are not sufficient for the appearance of Rad51 foci; Rad52, Rad55, and Rad57 are also required supporting a model in which these three proteins promote meiotic recombination by promoting the assembly of strand exchange complexes.

Links

PubMed PMC317010

Keywords

Adenosine Triphosphatases; Animals; DNA Repair Enzymes; DNA-Binding Proteins/metabolism; Fungal Proteins/metabolism; Meiosis; Rabbits; Rad51 Recombinase; Rad52 DNA Repair and Recombination Protein; Recombination, Genetic; Replication Protein A; S Phase; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


See also

References

See Help:References for how to manage references in GONUTS.