Terminal association of Rad54 protein with the Rad51-dsDNA filament

Konstantin Kiianitsa, Jachen A. Solinger, Wolf Dietrich Heyer

Research output: Contribution to journalArticle

42 Citations (Scopus)

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

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Homologous Recombination
Adenosine Triphosphatases
Rec A Recombinases
Proteins
Electron Microscopy
Hydrolysis
Adenosine Triphosphate
DNA
Enzymes

Keywords

  • ATPase
  • Recombination
  • Snf2-like proteins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Terminal association of Rad54 protein with the Rad51-dsDNA filament. / Kiianitsa, Konstantin; Solinger, Jachen A.; Heyer, Wolf Dietrich.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, No. 26, 27.06.2006, p. 9767-9772.

Research output: Contribution to journalArticle

Kiianitsa, Konstantin ; Solinger, Jachen A. ; Heyer, Wolf Dietrich. / Terminal association of Rad54 protein with the Rad51-dsDNA filament. In: Proceedings of the National Academy of Sciences of the United States of America. 2006 ; Vol. 103, No. 26. pp. 9767-9772.
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