Nucleic Acids Research, Vol 26, Issue 18 4146-4152, Copyright © 1998 by Oxford University Press
WL de Laat, AM Sijbers, H Odijk, NG Jaspers and JH Hoeijmakers
ERCC1-XPF is a heterodimeric protein complexinvolved in nucleotide excision
repair and recombinational processes. Like its homologous complex in
Saccharomyces cerevisiae , Rad10-Rad1, it acts as a structure-specific DNA
endonuclease, cleaving at duplex-single-stranded DNA junctions. In repair,
ERCC1-XPF and Rad10-Rad1 make an incision on the the 5'-side of the lesion.
No humans with a defect in the ERCC1 subunit of this protein complex have
been identified and ERCC1- deficient mice suffer from severe developmental
problems and signs of premature aging on top of a repair-deficient
phenotype. Xeroderma pigmentosum group F patients carry mutations in the
XPF subunit and generally show the clinical symptoms of mild DNA repair
deficiency. All XP-F patients examined demonstrate reduced levels of XPF
and ERCC1 protein, suggesting that proper complex formation is required for
stability of the two proteins. To better understand the molecular and
clinical consequences of mutations in the ERCC1-XPF complex, we decided to
map the interaction domains between the two subunits. The XPF- binding
domain comprises C-terminal residues 224-297 of ERCC1. Intriguingly, this
domain resides outside the region of homology with its yeast Rad10
counterpart. The ERCC1-binding domain in XPF maps to C- terminal residues
814-905. ERCC1-XPF complex formation is established by a direct interaction
between these two binding domains. A mutation from an XP-F patient that
alters the ERCC1-binding domain in XPF indeed affects complex formation
with ERCC1.
ARTICLES
Mapping of interaction domains between human repair proteins ERCC1 and XPF
Department of Cell Biology and Genetics, Medical Genetics Centre, Erasmus University, PO Box 1738,3000 DR Rotterdam, The Netherlands.
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