| Literature DB >> 7559382 |
C H Park1, T Bessho, T Matsunaga, A Sancar.
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.Entities:
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Year: 1995 PMID: 7559382 DOI: 10.1074/jbc.270.39.22657
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157