Logo image
Rad54 Protein Is Targeted to Pairing Loci by the Rad51 Nucleoprotein Filament
Journal article   Open access   Peer reviewed

Rad54 Protein Is Targeted to Pairing Loci by the Rad51 Nucleoprotein Filament

Alexander V Mazin, Carole J Bornarth, Jachen A Solinger, Wolf-Dietrich Heyer and Stephen C Kowalczykowski
Molecular cell, v 6(3), pp 583-592
2000
PMID: 11030338
url
https://doi.org/10.1016/S1097-2765(00)00057-5View
Published, Version of Record (VoR) Open

Abstract

Rad51 and Rad54 proteins are important for the repair of double-stranded DNA (dsDNA) breaks by homologous recombination in eukaryotes. Rad51 assembles on single-stranded DNA (ssDNA) to form a helical nucleoprotein filament that performs homologous pairing with dsDNA; Rad54 stimulates this pairing substantially. Here, we demonstrate that Rad54 acts in concert with the mature Rad51-ssDNA filament. Enhancement of DNA pairing by Rad54 is greatest at an equimolar ratio relative to Rad51 within the filament. Reciprocally, the Rad51-ssDNA filament enhances both the dsDNA-dependent ATPase and the dsDNA unwinding activities of Rad54. We conclude that Rad54 participates in the DNA homology search as a component of the Rad51-nucleoprotein filament and that the filament delivers Rad54 to the dsDNA pairing locus, thereby linking the unwinding of potential target DNA with the homology search process.

Metrics

7 Record Views
166 citations in Scopus

Details

UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

InCites Highlights

Data related to this publication, from InCites Benchmarking & Analytics tool:

Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
Logo image