Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease

C. H. Park, T. Bessho, T. Matsunaga, A. Sancar

Research output: Contribution to journalArticle

107 Scopus citations

Abstract

A complex, which consists of ERCC1 (38 kDa) and a 112-kDa protein, was purified from HeLa cells to homogeneity. This complex complemented the nucleotide excision repair defects of rodent ERCC-1, ERCC-4, and human XP-F mutant cell-free extracts, indicating that the 112-kDa protein is XPF/ERCC4 and providing direct biochemical evidence that XPF and ERCC4 are identical. The XPF/ERCC4-ERCC1 complex has an endonuclease activity with preference for single-stranded DNA and a single-stranded region of duplex DNA with a 'bubble' structure. This complex also nicks supercoiled DNA weakly, and this nicking activity is stimulated by human replication protein A when the DNA contains UV damage.

Original languageEnglish (US)
Pages (from-to)22657-22660
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number39
DOIs
StatePublished - Jan 1 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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