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 language | English (US) |
|---|---|
| Pages (from-to) | 22657-22660 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 270 |
| Issue number | 39 |
| DOIs | |
| State | Published - Jan 1 1995 |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease. / Park, C. H.; Bessho, T.; Matsunaga, T.; Sancar, A.
In: Journal of Biological Chemistry, Vol. 270, No. 39, 01.01.1995, p. 22657-22660.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease
AU - Park, C. H.
AU - Bessho, T.
AU - Matsunaga, T.
AU - Sancar, A.
PY - 1995/1/1
Y1 - 1995/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0029095693&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029095693&partnerID=8YFLogxK
U2 - 10.1074/jbc.270.39.22657
DO - 10.1074/jbc.270.39.22657
M3 - Article
C2 - 7559382
AN - SCOPUS:0029095693
VL - 270
SP - 22657
EP - 22660
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 39
ER -