Journal
NUCLEIC ACIDS RESEARCH
Volume 28, Issue 17, Pages 3206-3215Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/28.17.3206
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Funding
- NATIONAL CANCER INSTITUTE [R01CA078391, R56CA078391] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM035132] Funding Source: NIH RePORTER
- NCI NIH HHS [CA78391, R01 CA078391, R56 CA078391] Funding Source: Medline
- NIGMS NIH HHS [R01 GM035132, GM35132] Funding Source: Medline
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A protein homologous to the Escherichia coli MutY glycosylase, referred to as mtMYH, has been purified from calf liver mitochondria, SDS-polyacrylamide gel electrophoresis, western blot analysis as well as gel filtration chromatography predicted the molecular mass of the purified calf mtMYH to be 35-40 kDa, Gel mobility shift analysis showed that the purified mtMYH formed specific binding complexes with C/8-oxoG, G/8-oxoG and T/8-oxoG, weakly with C/8-oxoG, but not with A/G and A/C mismatches. The purified mtMYH exhibited DNA glycosylase activity removing adenine mispaired with G, C or 8-oxoG and weakly removing guanine mispaired with 8-oxoG, The mtMYH glycosylase activity was insensitive to high concentrations of NaCl and EDTA, The purified mtMYH cross-reacted with antibodies against both intact MutY and a peptide of human MutY homolog (hMYH). DNA glycosylase activity of mtMYH was inhibited by anti-MutY antibodies but not by anti-hMYH peptide antibodies. Together with the previously described mitochondrial MutT homolog (MTH1) and 8-oxoG glycosylase (OGG1, a functional MutM homolog), mtMYH can protect mitochondrial DNA from the mutagenic effects of 8-oxoG.
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