Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA

Stefan Sigurdsson, Kelly Trujillo, Bin Wei Song, Sabrina Stratton, Patrick Sung

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126 Scopus citations

Abstract

Human Rad51 (hRad51), a member of a conserved family of general recombinases, is shown here to have an avid capability to make DNA joints between homologous DNA molecules and promote highly efficient DNA strand exchange of the paired molecules over at least 5.4 kilobase pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric single-stranded DNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-single-stranded DNA nucleoprotein filament. The homologous DNA pairing and strand exchange system described should be valuable for dissecting the action mechanism of hRad51 and for deciphering its functional interactions with other recombination factors.

Original languageEnglish (US)
Pages (from-to)8798-8806
Number of pages9
JournalJournal of Biological Chemistry
Volume276
Issue number12
DOIs
Publication statusPublished - Mar 23 2001

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Sigurdsson, S., Trujillo, K., Song, B. W., Stratton, S., & Sung, P. (2001). Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA. Journal of Biological Chemistry, 276(12), 8798-8806. https://doi.org/10.1074/jbc.M010011200