PMID:7739614
| Citation |
Tajiri, T, Maki, H and Sekiguchi, M (1995) Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli. Mutat. Res. 336:257-67 |
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| Abstract |
8-Oxo-dGTP (8-oxo-7,8-dihydrodeoxyguanosine triphosphate) is a potent mutagenic substrate for DNA synthesis. The accumulation of 8-oxo-dGTP in the nucleotide pool induces G:C-->T:A transversion as well as A:T-->C:G transversion, and Escherichia coli cells possess mechanisms for preventing such mutations. The mutT gene product specifically hydrolyzes 8-oxo-dGTP to the monophosphate form while the mutM and the mutY gene products function to correct mispairs caused by incorporation of 8-oxoguanine into DNA. From analyses of forward mutations induced in cells lacking 8-oxo-dGTPase (MutT protein) and/or repair enzymes that suppress mutations caused by 8-oxoguanine in DNA (MutM and MutY proteins), cooperative functions of these proteins in control of the spontaneous mutagenesis became evident. In mutator strains lacking MutT and/or MutM proteins, 8-oxoguanine of DNA increased to a concentration expected from the increased rate of mutation. |
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| Keywords |
Bacterial Proteins/physiology; Base Sequence; DNA Glycosylases; DNA Repair/genetics; DNA Repair/physiology; DNA, Bacterial/metabolism; DNA-Formamidopyrimidine Glycosylase; Deoxyguanosine/analogs & derivatives; Deoxyguanosine/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Genes, Bacterial; Guanine/analogs & derivatives; Guanine/metabolism; Guanine Nucleotides/metabolism; Guanosine Triphosphate/metabolism; Molecular Sequence Data; N-Glycosyl Hydrolases/physiology; Oxidation-Reduction; Oxidative Stress/genetics; Phosphoric Monoester Hydrolases/physiology; Point Mutation; Pyrophosphatases; Suppression, Genetic; Templates, Genetic |
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