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PMID:7559382
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| Citation |
Park, CH, Bessho, T, Matsunaga, T and Sancar, A (1995) Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease. J. Biol. Chem. 270:22657-60 |
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| 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. |
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| Keywords |
Base Sequence; Chromatography, Affinity; DNA Repair; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/metabolism; Electrophoresis, Polyacrylamide Gel; Endonucleases; HeLa Cells; Humans; Molecular Sequence Data; Molecular Weight; Oligodeoxyribonucleotides; Proteins/isolation & purification; Proteins/metabolism; Substrate Specificity |
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