| Abstract: |
The Saccharomyces cerevisiae Swi2-like factors Rad54 and Rdh54 play multifaceted roles in homologous recombination via their DNA translocase activity. Aside from promoting Rad51-mediated DNA strand invasion of a partner chromatid, Rad54 and Rdh54 can remove Rad51 from duplex DNA for intracellular recycling. Although the in vitro properties of the two proteins are similar, differences between the phenotypes of the null allele mutants suggest that they play different roles in vivo. Through the isolation of a novel RAD51 allele encoding a protein with reduced affinity for DNA, we provide evidence that Rad54 and Rdh54 have different in vivo interactions with Rad51. The mutant Rad51 forms a complex on duplex DNA that is more susceptible to dissociation by Rdh54. This Rad51 variant distinguishes the in vivo functions of Rad54 and Rdh54, leading to the conclusion that two translocases remove Rad51 from different substrates in vivo. Additionally, we show that a third Swi2-like factor, Uls1, contributes toward Rad51 clearance from chromatin in the absence of Rad54 and Rdh54, and define a hierarchy of action of the Swi2-like translocases for chromosome damage repair. © 2011 The Author(s). |
| Keywords: |
controlled study; unclassified drug; genetics; mutation; nonhuman; binding affinity; protein function; metabolism; dna repair; protein dna binding; protein protein interaction; in vivo study; physiology; chemistry; dna; saccharomyces cerevisiae; dna repair enzymes; rad54 protein; helicase; yeast; saccharomyces cerevisiae proteins; saccharomyces cerevisiae protein; polydeoxyribonucleotide synthase; dna helicases; rad51 protein; mutant; dna topoisomerase; fungal gene; rad51 recombinase; nucleic acid binding protein; dna protein complex; suppressor gene; gene isolation; genes, suppressor; dna topoisomerases; rad51 protein, s cerevisiae; rad54 protein, s cerevisiae; rdh54 protein, s cerevisiae; ris1 protein, s cerevisiae; protein rdh54; protein uls1; rad51 gene
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