PMID:1309939

Citation	Maki, H and Sekiguchi, M (1992) MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature 355:273-5
Abstract	Errors in the replication of DNA are a major source of spontaneous mutations, and a number of cellular functions are involved in correction of these errors to keep the frequency of spontaneous mutations very low. We report here a novel mechanism which prevents replicational errors by degrading a potent mutagenic substrate for DNA synthesis. This error-avoiding process is catalysed by a protein encoded by the mutT gene of Escherichia coli, mutations of which increase the occurrence of A.T----C.G transversions 100 to 10,000 times the level of the wild type. Spontaneous oxidation of dGTP forms 8-oxo-7,8-dihydro-2'-dGTP (8-oxodGTP), which is inserted opposite dA and dC residues of template DNA with almost equal efficiency, and the MutT protein specifically degrades 8-oxodGTP to the monophosphate. This indicates that elimination from the nucleotide pool of the oxidized form of guanine nucleotide is important for the high fidelity of DNA synthesis.
Links	PubMed Online version:10.1038/355273a0
Keywords	Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Composition; Base Sequence; DNA Replication; Deoxyadenine Nucleotides/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Hydrolysis; Kinetics; Molecular Sequence Data; Mutation; Phosphoric Monoester Hydrolases/metabolism; Pyrophosphatases; Substrate Specificity; Templates, Genetic
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