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

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

Research output: Contribution to journalArticle

104 Citations (Scopus)

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

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DNA Repair
Purification
Repair
Superhelical DNA
Endonucleases
Single-Stranded DNA
DNA
Cell Extracts
HeLa Cells
Rodentia
Proteins
Nucleotides
Defects
human RPA1 protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease. / Park, C. H.; Bessho, Tadayoshi; Matsunaga, T.; Sancar, A.

In: Journal of Biological Chemistry, Vol. 270, No. 39, 01.01.1995, p. 22657-22660.

Research output: Contribution to journalArticle

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