Nucleic Acids Research, Vol 25, Issue 3 474-479, Copyright © 1997 by Oxford University Press
A Karakaya, P Jaruga, VA Bohr, AP Grollman and M Dizdaroglu
The kinetics of excision of damaged purine bases from oxidatively damaged
DNA by Escherichia coli Fpg protein were investigated. DNA substrates,
prepared by treatment with H2O2/Fe(III)-EDTA or by gamma- irradiation under
N2O or air, were incubated with Fpg protein, followed by precipitation of
DNA. Precipitated DNA and supernatant fractions were analyzed by gas
chromatography/isotope-dilution mass spectrometry. Kinetic studies revealed
efficient excision of 8-hydroxyguanine (8-OH- Gua),
2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) and 4, 6-
diamino-5-formamidopyrimidine (FapyAde). Thirteen other modified bases in
the oxidized DNA substrates, including 5-hydroxycytosine and 5-
hydroxyuracil, were not excised. Excision was measured as a function of
enzyme concentration, substrate concentration, time and temperature. The
rate of release of modified purine bases from the three damaged DNA
substrates varied significantly even though each DNA substrate contained
similar levels of oxidative damage. Specificity constants (kcat/KM) for the
excision reaction indicated similar preferences of Fpg protein for excision
of 8-OH-Gua, FapyGua and FapyAde from each DNA substrate. These findings
suggest that, in addition to 8-OH-Gua, FapyGua and FapyAde may be primary
substrates for this enzyme in cells.
ARTICLES
Kinetics of excision of purine lesions from DNA by Escherichia coli Fpg protein
Chemical Science and Technology Laboratory, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA.
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