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• W2143669378 startingPage "6151" @default.
• W2143669378 abstract "ABSTRACT The mutY homolog gene ( mutY Dr ) from Deinococcus radiodurans encodes a 39.4-kDa protein consisting of 363 amino acids that displays 35% identity to the Escherichia coli MutY (MutY Ec ) protein. Expressed MutY Dr is able to complement E. coli mutY mutants but not mutM mutants to reduce the mutation frequency. The glycosylase and binding activities of MutY Dr with an A/G-containing substrate are more sensitive to high salt and EDTA concentrations than the activities with an A/7,8-dihydro-8-oxoguanine (GO)-containing substrate are. Like the MutY Ec protein, purified recombinant MutY Dr expressed in E. coli has adenine glycosylase activity with A/G, A/C, and A/GO mismatches and weak guanine glycosylase activity with a G/GO mismatch. However, MutY Dr exhibits limited apurinic/apyrimidinic lyase activity and can form only weak covalent protein-DNA complexes in the presence of sodium borohydride. This may be due to an arginine residue that is present in MutY Dr at the position corresponding to the position of MutY Ec Lys142, which forms the Schiff base with DNA. The kinetic parameters of MutY Dr are similar to those of MutY Ec . Although MutY Dr has similar substrate specificity and a binding preference for an A/GO mismatch over an A/G mismatch, as MutY Ec does, the binding affinities for both mismatches are slightly lower for MutY Dr than for MutY Ec . Thus, MutY Dr can protect the cell from GO mutational effects caused by ionizing radiation and oxidative stress." @default.
• W2143669378 created "2016-06-24" @default.
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• W2143669378 date "2001-11-01" @default.
• W2143669378 modified "2023-10-12" @default.
• W2143669378 title "Molecular Cloning and Functional Analysis of the MutY Homolog of Deinococcus radiodurans" @default.
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• W2143669378 doi "https://doi.org/10.1128/jb.183.21.6151-6158.2001" @default.
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