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(Received for publication, April 30, 1997, and in revised form, July 30, 1997)
From the Reactive oxygen species have been shown to
generate mutagenic lesions in DNA. One of the most abundant lesions in
both nuclear and mitochondrial DNA is 7,8-dihydro-8-oxoguanine
(8-oxoG). We report here the partial purification and characterization
of a mitochondrial oxidative damage endonuclease (mtODE) from rat liver that recognizes and incises at 8-oxoG and abasic sites in duplex DNA.
Rat liver mitochondria were purified by differential and Percoll
gradient centrifugation, and mtODE was extracted from Triton
X-100-solubilized mitochondria. Incision activity was measured using a
radiolabeled double-stranded DNA oligonucleotide containing a unique
8-oxoG, and reaction products were separated by polyacrylamide gel
electrophoresis. Gel filtration chromatography predicts mtODE's molecular mass to be between 25 and 30 kDa. mtODE has a monovalent cation optimum between 50 and 100 mM KCl and a pH
optimum between 7.5 and 8. mtODE does not require any co-factors and is
active in the presence of 5 mM EDTA. It is specific for
8-oxoG and preferentially incises at 8-oxoG:C base pairs. mtODE is a
putative 8-oxoG glycosylase/lyase enzyme, because it can be covalently
linked to the 8-oxoG oligonucleotide by sodium borohydride reduction.
Comparison of mtODE's activity with other known 8-oxoG
glycosylases/lyases and mitochondrial enzymes reveals that this may be
a novel protein.
Volume 272, Number 43,
Issue of October 24, 1997
pp. 27338-27344
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
An Oxidative Damage-specific Endonuclease from Rat Liver
Mitochondria
§
,
,
,
,
and
Laboratory of Molecular Genetics, NIA,
National Institutes of Health, Baltimore, Maryland 21224 and the
§ Department of Pharmacology and Molecular Sciences, Johns
Hopkins University, Baltimore, Maryland 21205
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