RAD54 controls access to the invading 3′-OH end after RAD51-mediated DNA strand invasion in homologous recombination in Saccharomyces cerevisiae

Xuan Li, Wolf Dietrich Heyer

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

Rad51 is a key protein in homologous recombination performing homology search and DNA strand invasion. After DNA strand exchange Rad51 protein is stuck on the double-stranded heteroduplex DNA product of DNA strand invasion. This is a problem, because DNA polymerase requires access to the invading 3′-OH end to initiate DNA synthesis. Here we show that, the Saccharomyces cerevisiae dsDNA motor protein Rad54 solves this problem by dissociating yeast Rad51 protein bound to the heteroduplex DNA after DNA strand invasion. The reaction required species-specific interaction between both proteins and the ATPase activity of Rad54 protein. This mechanism rationalizes the in vivo requirement of Rad54 protein for the turnover of Rad51 foci and explains the observed dependence of the transition from homologous pairing to DNA synthesis on Rad54 protein in vegetative and meiotic yeast cells.

Original languageEnglish (US)
Pages (from-to)638-646
Number of pages9
JournalNucleic Acids Research
Volume37
Issue number2
DOIs
StatePublished - 2009

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Homologous Recombination
Saccharomyces cerevisiae
DNA
Nucleic Acid Heteroduplexes
Proteins
Fungal Proteins
DNA-Directed DNA Polymerase
Adenosine Triphosphatases
Yeasts

ASJC Scopus subject areas

  • Genetics

Cite this

RAD54 controls access to the invading 3′-OH end after RAD51-mediated DNA strand invasion in homologous recombination in Saccharomyces cerevisiae. / Li, Xuan; Heyer, Wolf Dietrich.

In: Nucleic Acids Research, Vol. 37, No. 2, 2009, p. 638-646.

Research output: Contribution to journalArticle

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