Nucleic Acids Research, Vol 27, Issue 20 4001-4007, Copyright © 1999 by Oxford University Press
C Dherin, JP Radicella, M Dizdaroglu and S Boiteux
We have investigated the substrate specificity of the major nuclear form of
the human Ogg1 protein, referred as alpha-hOgg1, for excision of damaged
bases from DNA exposed to gamma-irradiation. Excision products were
identified and quantified using gas chromatography/isotope dilution mass
spectrometry (GC/IDMS). The GST- alpha-hOgg1 protein used in this study is
a fusion of alpha-hOgg1 to the C-terminus of the GST protein. The results
show that GST-alpha- hOgg1 protein excises 8-hydroxyguanine (8-OH-Gua) and
2,6-diamino-4- hydroxy-5-formamidopyrimidine (FapyGua) from DNA exposed to
gamma- irradiation in a solution saturated with N(2)O or air. Fourteen
other lesions, including oxidised purines and pyrimidines, were not excised
from these substrates. Catalytic constants were measured for the excision
of 8-OH-Gua and FapyGua from DNA gamma-irradiated under N(2)O. The k (cat)/
K (m)values for excision of 8-OH-Gua and FapyGua were 4.47 x 10(-5)and 8.97
x 10(-5)(min(-1)nM(-1)), respectively. The substrate specificity and the
catalytic parameters of the wild-type GST-alpha- hOgg1 protein were
compared to that of a polymorphic form of alpha- hOgg1 harbouring a
Ser-->Cys mutation at codon 326. In the Japanese population, 47.6% of
individuals possess both alleles coding for the wild-type
alpha-hOgg1-Ser(326)and mutant alpha-hOgg1-Cys(326)proteins. The
GST-alpha-hOgg1-Cys(326)protein was purified and its substrate specificity
was determined by GC/IDMS analysis. The results show that the
GST-alpha-hOgg1-Cys(326)protein efficiently excises 8-OH-Gua and FapyGua
from gamma-irradiated DNA. The k (cat)/ K (m)values for excision of
8-OH-Gua and FapyGua were 2. 82 x 10(-5)and 4.43 x 10(- 5)(min(-1)nM(-1)),
respectively. Furthermore, we compared the capacity of these two forms of
alpha-hOgg1 to act on substrates containing 2,6- diamino-4-hydroxy-5- N
-methylformamidopyrimidine (Me-FapyGua). The k (cat)/ K (m)values for
excision of Me-FapyGua were 278 x 10(-5)and 319 x 10(-5)(min(-1)nM(-1)),
respectively. Cleavage of 34mer oligodeoxyribonucleotides containing
8-OH-Gua, 8-hydroxyadenine or an apurinic/apyrimidinic site paired with a
cytosine was also investigated. The results show that both
GST-alpha-hOgg1-Ser(326)and GST-alpha-hOgg1-Cys(326)catalyse the various
cleavage reactions at very similar rates. Furthermore, both proteins
efficiently complement the mutator phenotype of the fpg mutY mutant of
Escherichia coli.
ARTICLES
Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations
CEA, DSV, DRR, UMR217 CNRS-CEA, Radiobiologie Moleculaire et Cellulaire, Fontenay aux Roses, France.
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