Terminal association of Rad54 protein with the Rad51-dsDNA filament

Konstantin Kiianitsa, Jachen A. Solinger, Wolf Dietrich Heyer

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

Rad54 protein is a Snf2-related dsDNA-specific ATPase essential for homologous recombination mediated by Rad51 protein, the eukaryotic RecA ortholog. Snf2-related enzymes couple ATP hydrolysis with translocation on dsDNA to remodel or dissociate a wide variety of protein-dsDNA complexes. Rad54 and Rad51 interact through species-specific contacts and mutually stimulate their biochemical activities. Specifically, Rad51 bound to dsDNA, the product of homologous recombination after DNA-strand exchange, stimulates the Rad54 ATPase up to 6-fold, leading to the turnover of Rad51 in the product complex. Electron microscopy visualized the Rad51-Rad54 interaction on dsDNA, showing that an oligomeric form of Rad54 associates preferentially with termini of the Rad51-dsDNA filament. Our data support a mechanism of processive dsDNA-RadS1 filament dissociation by the translocating Rad54 protein.

Original languageEnglish (US)
Pages (from-to)9767-9772
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume103
Issue number26
DOIs
StatePublished - Jun 27 2006

Keywords

  • ATPase
  • Recombination
  • Snf2-like proteins

ASJC Scopus subject areas

  • Genetics
  • General

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