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Genetics, Vol. 168, 1219-1230, November 2004, Copyright © 2004
doi:10.1534/genetics.103.025700

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The Budding Yeast Mei5 and Sae3 Proteins Act Together With Dmc1 During Meiotic Recombination

Hideo Tsubouchi* and G. Shirleen Roeder*,{dagger},1

* Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520-8103
{dagger} Department of Molecular, Cellular and Developmental Biology and Department of Genetics, Yale University, New Haven, Connecticut 06520-8103

1 Corresponding author: Howard Hughes Medical Institute, Department of Molecular, Cellular and Developmental Biology, Yale University, P.O. Box 208103, 266 Whitney Ave., New Haven, CT 06520-8103.
E-mail: shirleen.roeder{at}yale.edu

Here we provide evidence that the Mei5 and Sae3 proteins of budding yeast act together with Dmc1, a meiosis-specific, RecA-like recombinase. The mei5 and sae3 mutations reduce sporulation, spore viability, and crossing over to the same extent as dmc1. In all three mutants, these defects are largely suppressed by overproduction of Rad51. In addition, mei5 and sae3, like dmc1, suppress the cell-cycle arrest phenotype of the hop2 mutant. The Mei5, Sae3, and Dmc1 proteins colocalize to foci on meiotic chromosomes, and their localization is mutually dependent. The localization of Rad51 to chromosomes is not affected in either mei5 or sae3. Taken together, these observations suggest that the Mei5 and Sae3 proteins are accessory factors specific to Dmc1. We speculate that Mei5 and Sae3 are necessary for efficient formation of Dmc1-containing nucleoprotein filaments in vivo.




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