Physical and Functional Interaction between the XPF/ERCC1 Endonuclease and hRad52

Teresa A. Motycka, Tadayoshi Bessho, Sean M. Post, Patrick Sung, Alan E. Tomkinson

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

The XPF/ERCC1 heterodimer is a DNA structure-specific endonuclease that participates in nucleotide excision repair and homology-dependent recombination reactions, including DNA single strand annealing and gene targeting. Here we show that XPF/ERCC1 is stably associated with hRad52, a recombinational repair protein, in human cell-free extracts and that these factors interact directly via the N-terminal domain of hRad52 and the XPF protein. Complex formation between hRad52 and XPF/ERCC1 concomitantly stimulates the DNA structure-specific endonuclease activity of XPF/ ERCC1 and attenuates the DNA strand annealing activity of hRad52. Our results reveal a novel role for hRad52 as a subunit of a DNA structure-specific endonuclease and are congruent with evidence implicating both hRad52 and XPF/ERCC1 in a number of homologous recombination reactions. We propose that the ternary complex of hRad52 and XPF/ERCC1 is the active species that processes recombination intermediates generated during the repair of DNA double strand breaks and in homology-dependent gene targeting events.

Original languageEnglish (US)
Pages (from-to)13634-13639
Number of pages6
JournalJournal of Biological Chemistry
Volume279
Issue number14
DOIs
StatePublished - Apr 2 2004

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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