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doi:10.1534/genetics.105.047845
A more recent version of this article appeared on January 1, 2006.
REGULAR RESEARCH PAPERS |
Evidence of Meiotic Crossover Control in Saccharomyces cerevisiae through Mec1-mediated Phosphorylation of Replication Protein A
Amy J. Bartrand 1, Dagmawi Iyasu 1, Suzanne M. Marinco 1 and George S. Brush 1*
1 Karmanos Cancer Institute
* To whom correspondence should be addressed. E-mail: brushg{at}karmanos.org.
Submitted on July 6, 2005
Revised on August 2, 2005
Accepted on 2 August 2005
Replication protein A (RPA) is the major single-stranded DNA-binding protein in eukaryotes, essential for DNA replication, repair, and recombination. During mitosis and meiosis in budding yeast, RPA becomes phosphorylated in reactions that require the Mec1 protein kinase, a central checkpoint regulator and homologue of human ATR. Through mass spectrometry and site-directed mutagenesis, we have now identified a single serine residue in the middle subunit of the RPA heterotrimer that is targeted for phosphorylation by Mec1 both in vivo and in vitro. Cells containing a phosphomimetic version of RPA generated by mutation of this serine to aspartate exhibit a significant alteration in the pattern of meiotic crossovers for specific genetic intervals. These results suggest a new function of Mec1 that operates through RPA to locally control reciprocal recombination.
Key Words: Mec1, interference, meiosis, recombination, replication protein A
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