Synergistic action of the Saccharomyces cerevisiae homologous recombination factors Rad54 and Rad51 in chromatin remodeling

Rad54, a member of the Swi2/Snf2 protein family, works in concert with the RecA-like recombinase Rad51 during the early and late stages of homologous recombination. Rad51 markedly enhances the activities of Rad54, including the induction of topological changes in DNA and the remodeling of chromatin...

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Bibliographic Details
Published in:DNA repair 2007-10, Vol.6 (10), p.1496-1506
Main Authors: Kwon, YoungHo, Chi, Peter, Roh, Dong Hyun, Klein, Hannah, Sung, Patrick
Format: Article
Language:English
Subjects:
Bacteriology
Biological and medical sciences
Chromatin - metabolism
Chromatin remodeling
Chromatin. Chromosome
D-loop
DNA Helicases
DNA Repair Enzymes
Fundamental and applied biological sciences. Psychology
Growth, nutrition, cell differenciation
Homologous recombination
Microbiology
Molecular and cellular biology
Molecular genetics
Mutagenesis. Repair
Mutation
Rad51
Rad51 Recombinase - genetics
Rad51 Recombinase - physiology
Rad54
Recombination, Genetic
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - physiology
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Summary:Rad54, a member of the Swi2/Snf2 protein family, works in concert with the RecA-like recombinase Rad51 during the early and late stages of homologous recombination. Rad51 markedly enhances the activities of Rad54, including the induction of topological changes in DNA and the remodeling of chromatin structure. Reciprocally, Rad54 promotes Rad51-mediated DNA strand invasion with either naked or chromatinized DNA. Here, using various Saccharomyces cerevisiae rad51 and rad54 mutant proteins, mechanistic aspects of Rad54/Rad51-mediated chromatin remodeling are defined. Disruption of the Rad51–Rad54 complex leads to a marked attenuation of chromatin remodeling activity. Moreover, we present evidence that assembly of the Rad51 presynaptic filament represents an obligatory step in the enhancement of the chromatin remodeling reaction. Interestingly, we find a specific interaction of the N-terminal tail of histone H3 with Rad54 and show that the H3 tail interaction domain resides within the amino terminus of Rad54. These results suggest that Rad54-mediated chromatin remodeling coincides with DNA homology search by the Rad51 presynaptic filament and that this process is facilitated by an interaction of Rad54 with histone H3.
ISSN:1568-7864
1568-7856
DOI:10.1016/j.dnarep.2007.04.012