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• W2077893595 startingPage "586" @default.
• W2077893595 abstract "Meiotic homologous recombination in Saccharomyces cerevisiae involves formation of nucleoprotein filaments of Rad51 and Dmc1 that mediate DNA strand exchange between homologous chromosomes. The Mei5-Sae3 protein complex functions as a recombination mediator to promote nucleation of the Dmc1 recombinase onto replication protein A-coated single-stranded DNA. Here, we have expressed and purified the Mei5 protein, Sae3 protein and the Mei5-Sae3 complex for biochemical studies. We show the Mei5-Sae3 complex preferentially binds a fork-like DNA substrate to 3' overhanging DNA, single-stranded DNA or double-stranded DNA. We demonstrate that Mei5 confers DNA binding activity to the Mei5-Sae3 complex. We determined Mei5-Sae3 interacts with the Rad51 recombinase through the N-terminal domain of Mei5. Unlike Rad52, Mei5-Sae3 lacks recombination mediator activity for Rad51. Importantly, we find that the Mei5-Sae3 complex does not harbor single-strand DNA annealing activity. These properties of the Mei5-Sae3 complex distinguishes it from the Rad52 protein, which serves as the mediator of Rad51 and is involved in the single-strand DNA annealing pathway of homologous recombination." @default.
• W2077893595 created "2016-06-24" @default.
• W2077893595 creator A5030034693 @default.
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• W2077893595 date "2011-06-01" @default.
• W2077893595 modified "2023-10-06" @default.
• W2077893595 title "The budding yeast Mei5–Sae3 complex interacts with Rad51 and preferentially binds a DNA fork structure" @default.
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• W2077893595 doi "https://doi.org/10.1016/j.dnarep.2011.03.006" @default.
• W2077893595 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3119066" @default.
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