TY - JOUR
T1 - Repair of an interstrand DNA cross-link initiated by ERCC1-XPF repair/recombination nuclease
AU - Kuraoka, Isao
AU - Kobertz, William R.
AU - Ariza, Rafael R.
AU - Biggerstaff, Maureen
AU - Essigmann, John M.
AU - Wood, Richard D.
PY - 2000/8/25
Y1 - 2000/8/25
N2 - Interstrand DNA cross-link damage is a severe challenge to genomic integrity. Nucleotide excision repair plays some role in the repair of DNA cross-links caused by psoralens and other agents. However, in mammalian ceils there is evidence that the ERCC1-XPF nuclease has a specialized additional function during interstrand DNA cross-link repair, beyond its role in nucleotide excision repair. We placed a psoralen monoadduct or interstrand cross-link in a duplex, 4-6 bases from a junction with unpaired DNA. ERCC1-XPF endonucleo-lytically cleaved within the duplex on either side of the adduct, on the strand having an unpaired 3' tail. Crosslinks that were cleaved only on the 5' side were purified and reincubated with ERCC1-XPF. A second cleavage was then observed on the 3' side. Relevant partially unwound structures near a cross-link may be expected to arise frequently, for example at stalled DNA replication forks. The results show that the single enzyme ERCC1-XPF can release one arm of a cross-link and suggest a novel mechanism for interstrand cross-link repair.
AB - Interstrand DNA cross-link damage is a severe challenge to genomic integrity. Nucleotide excision repair plays some role in the repair of DNA cross-links caused by psoralens and other agents. However, in mammalian ceils there is evidence that the ERCC1-XPF nuclease has a specialized additional function during interstrand DNA cross-link repair, beyond its role in nucleotide excision repair. We placed a psoralen monoadduct or interstrand cross-link in a duplex, 4-6 bases from a junction with unpaired DNA. ERCC1-XPF endonucleo-lytically cleaved within the duplex on either side of the adduct, on the strand having an unpaired 3' tail. Crosslinks that were cleaved only on the 5' side were purified and reincubated with ERCC1-XPF. A second cleavage was then observed on the 3' side. Relevant partially unwound structures near a cross-link may be expected to arise frequently, for example at stalled DNA replication forks. The results show that the single enzyme ERCC1-XPF can release one arm of a cross-link and suggest a novel mechanism for interstrand cross-link repair.
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U2 - 10.1074/jbc.C000337200
DO - 10.1074/jbc.C000337200
M3 - Article
C2 - 10882712
AN - SCOPUS:0034714401
SN - 0021-9258
VL - 275
SP - 26632
EP - 26636
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 34
ER -