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Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51-ssDNA nucleoprotein filament
Journal article   Peer reviewed

Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51-ssDNA nucleoprotein filament

Andrei Alexeev, Alexander Mazin and Stephen C Kowalczykowski
Nature structural biology, v 10(3), pp 182-186
Mar 2003
PMID: 12577053

Abstract

Chromatin - metabolism Actin Cytoskeleton - metabolism Rad51 Recombinase Saccharomyces cerevisiae - genetics DNA, Single-Stranded - metabolism Nucleoproteins - genetics Nucleosomes - metabolism Saccharomyces cerevisiae Proteins - genetics DNA Repair Enzymes DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Saccharomyces cerevisiae - metabolism DNA Helicases Biological Transport Nucleoproteins - metabolism Recombination, Genetic DNA Repair Saccharomyces cerevisiae Proteins - metabolism Microfilament Proteins - metabolism
In Saccharomyces cerevisiae, the Rad54 protein participates in the recombinational repair of double-strand DNA breaks together with the Rad51, Rad52, Rad55 and Rad57 proteins. In vitro, Rad54 interacts with Rad51 and stimulates DNA strand exchange promoted by Rad51 protein. Rad54 is a SWI2/SNF2-related protein that possesses double-stranded DNA-dependent ATPase activity and changes DNA topology in an ATP hydrolysis-dependent manner. Here we show that Rad54 catalyzes bidirectional nucleosome redistribution by sliding nucleosomes along DNA. Nucleosome redistribution is greatly stimulated by the Rad51 nucleoprotein filament but does not require the presence of homologous single-stranded DNA within the filament. On the basis of these data, we propose that Rad54 facilitates chromatin remodeling and, perhaps more generally, protein clearing at the homology search step of genetic recombination.

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Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
Cell Biology
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