Association of Mre11p with double-strand break sites during yeast meiosis Journal Article


Authors: Borde, V.; Lin, W.; Novikov, E.; Petrini, J. H.; Lichten, M.; Nicolas, A.
Article Title: Association of Mre11p with double-strand break sites during yeast meiosis
Abstract: The repair of DNA double-strand breaks (DSBs) requires the activity of the Mre11/Rad50/Xrs2(Nbs1) complex. In Saccharomyces cerevisiae, this complex is required for both the initiation of meiotic recombination by Spo11p-catalyzed programmed DSBs and for break end resection, which is necessary for repair by homologous recombination. We report that Mre11p transiently associates with the chromatin of Spo11-dependent DSB regions throughout the genome. Mutant analyses show that Mre11p binding requires the function of all genes required for DSB formation, with the exception of RAD50. However, Mre11p binding does not require DSB formation itself, since Mre11p transiently associates with DSB regions in the catalysis-negative mutant spo11-Y135F. Mre11p release from chromatin is blocked in mutants that accumulate unresected DSBs. We propose that Mre11p is a component of a pre-DSB complex that assembles on the DSB sites, thus ensuring a tight coupling between DSB formation by Spo11p and the processing of break ends.
Keywords: controlled study; unclassified drug; dna binding protein; genetics; mutation; dna-binding proteins; nonhuman; protein localization; meiosis; metabolism; mre11 protein; rad50 protein; dna damage; cells, cultured; dna repair; protein binding; gene function; mutational analysis; wild type; dna strand breakage; dna; double stranded dna; cell culture; saccharomyces cerevisiae; chromatin; protein secretion; chromosome breakage; binding site; binding sites; yeast; saccharomyces cerevisiae proteins; catalysis; saccharomyces cerevisiae protein; cell mutant; spo11 protein; esterase; macromolecule; esterases; macromolecular substances; fungal gene; deoxyribonuclease; exodeoxyribonuclease; endodeoxyribonucleases; exodeoxyribonucleases; saccharomyces; article; mre11 protein, s cerevisiae; rad50 protein, s cerevisiae
Journal Title: Molecular Cell
Volume: 13
Issue: 3
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 2004-02-13
Start Page: 389
End Page: 401
Language: English
DOI: 10.1016/s1097-2765(04)00034-6
PROVIDER: scopus
PUBMED: 14967146
DOI/URL:
Notes: Mol. Cell -- Cited By (since 1996):89 -- Export Date: 16 June 2014 -- CODEN: MOCEF -- Source: Scopus
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  1. John Petrini
    84 Petrini