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Rad51 protein stimulates the branch migration activity of Rad54 protein
Journal article   Open access   Peer reviewed

Rad51 protein stimulates the branch migration activity of Rad54 protein

Matthew J Rossi and Alexander V Mazin
The Journal of biological chemistry, v 283(36), pp 24698-24706
05 Sep 2008
PMID: 18617519
url
https://doi.org/10.1074/jbc.M800839200View
Published, Version of Record (VoR) Open

Abstract

Recombination, Genetic - physiology Saccharomyces cerevisiae - genetics Humans DNA, Cruciform - metabolism DNA, Single-Stranded - genetics Saccharomyces cerevisiae - metabolism Nuclear Proteins - genetics DNA, Cruciform - genetics DNA-Binding Proteins Rad51 Recombinase - metabolism Recombinant Proteins - metabolism Rad51 Recombinase - genetics DNA, Single-Stranded - metabolism Recombinant Proteins - chemistry Nuclear Proteins - metabolism Recombinant Proteins - genetics Saccharomyces cerevisiae Proteins - genetics Nuclear Proteins - chemistry DNA, Single-Stranded - chemistry Saccharomyces cerevisiae - chemistry DNA Helicases Rad51 Recombinase - chemistry Saccharomyces cerevisiae Proteins - metabolism DNA, Cruciform - chemistry Evolution, Molecular Saccharomyces cerevisiae Proteins - chemistry
The Rad51 and Rad54 proteins play important roles during homologous recombination in eukaryotes. Rad51 forms a nucleoprotein filament on single-stranded DNA and performs the initial steps of double strand break repair. Rad54 belongs to the Swi2/Snf2 family of ATP-dependent DNA translocases. We previously showed that Rad54 promotes branch migration of Holliday junctions. Here we find that human Rad51 (hRad51) significantly stimulates the branch migration activity of hRad54. The stimulation appears to be evolutionarily conserved, as yeast Rad51 also stimulates the branch migration activity of yeast Rad54. We further investigated the mechanism of this stimulation. Our results demonstrate that the stimulation of hRad54-promoted branch migration by hRad51 is driven by specific protein-protein interactions, and the active form of the hRad51 filament is more stimulatory than the inactive one. The current results support the hypothesis that the hRad51 conformation state has a strong effect on interaction with hRad54 and ultimately on the function of hRad54 in homologous recombination.

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Web of Science research areas
Biochemistry & Molecular Biology
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