Rad54 protein is targeted to pairing loci by the Rad51 nucleoprotein filament

Alexander V. Mazin, Carole J. Bornarth, Jachen A. Solinger, Wolf Dietrich Heyer, Stephen C. Kowalczykowski

Research output: Contribution to journalArticlepeer-review

163 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)583-592
Number of pages10
JournalMolecular Cell
Volume6
Issue number3
DOIs
StatePublished - 2000
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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