Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange

Stefan Sigurdsson, Stephen Van Komen, Wendy Bussen, David Schild, Joanna S. Albala, Patrick Sung

Research output: Contribution to journalArticlepeer-review

168 Scopus citations

Abstract

Five Rad51-like proteins, referred to as Rad51 paralogs, have been described in vertebrates. We show that two of them, Rad51B and Rad51C, are associated in a stable complex. Rad51B-Rad51C complex has ssDNA binding and ssDNA-stimulated ATPase activities. We also examined the functional interaction of Rad51B-Rad51C with Rad51 and RPA. Even though RPA enhances Rad51-catalyzed DNA joint formation via removal of secondary structure in the ssDNA substrate, it can also compete with Rad51 for binding to the substrate, leading to suppressed reaction efficiency. The competition by RPA for substrate binding can be partially alleviated by Rad51B-Rad51C. This recombination mediator function of Rad51B-Rad51C is likely required for the assembly of the Rad51-ssDNA nucleoprotein filament in vivo.

Original languageEnglish (US)
Pages (from-to)3308-3318
Number of pages11
JournalGenes and Development
Volume15
Issue number24
DOIs
StatePublished - Dec 15 2001

Keywords

  • DNA double-strand break repair
  • Tumor suppression

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

Fingerprint Dive into the research topics of 'Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange'. Together they form a unique fingerprint.

Cite this