Nucleic Acids Research, Vol 26, Issue 20 4662-4668, Copyright © 1998 by Oxford University Press
T Kobayashi, S Takeuchi, M Saijo, Y Nakatsu, H Morioka, E Otsuka, M Wakasugi, O Nikaido and K Tanaka
To analyze the function of the xeroderma pigmentosum group A (XPA) protein
in strand-specific DNA repair, we examined repair of UV-induced cyclobutane
pyrimidine dimer (CPD) in transcribed and non-transcribed strands of the
dihydrofolate reductase gene of xeroderma pigmentosum group A (XP-A) cell
line (XP12ROSV) which was transfected with various types of mutant XPA
cDNA. The transfectant overexpressing mutant XPA with a defect in the
interaction with either ERCC1, replication protein A (RPA), or general
transcription factor TFIIH, showed more or less decreased repair of CPD in
each strand in parallel, while in the transfectant overexpressing R207G
(Arg207to Gly) mutant XPA derived from XP129, a UV-resistant XP12ROSV
revertant, the rate of CPD repair was almost normal in each strand. We also
examined the dose responses of the XPA protein on CPD repair in each strand
by the modulation of the expression levels of wild-type or R207G mutant XPA
using an inducible expression system, LacSwitchtrade mark promoter. There
were good correlations between the rate of CPD repair in each strand and
the amount of XPA protein produced in these Lac cells. Our results indicate
that the XPA protein is equally important for the CPD repair in both
transcribed and non-transcribed strands and that the R207G mutation found
in XP129 may not be responsible for a selective defect in CPD repair in the
non-transcribed strand in XP129.
ARTICLES
Mutational analysis of a function of xeroderma pigmentosum group A (XPA) protein in strand-specific DNA repair
Institute for Molecular and Cellular Biology, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
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