PMID:2682664
| Citation |
Au, KG, Clark, S, Miller, JH and Modrich, P (1989) Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. U.S.A. 86:8877-81 |
|---|---|
| Abstract |
Mutations in the mutY gene of Escherichia coli confer hypermutability reflecting G.C to T.A transversion mutations and result in a deficiency in methyl-independent G-A to G.C mismatch correction. In the present work, the mutY product has been purified to near homogeneity by virtue of its ability to restore G-A to G.C mismatch correction to cell-free extracts of a mutS mutY strain. The 36-kDa protein renders the strand containing the mispaired adenine labile to base-catalyzed cleavage and sensitive to cleavage by several apurinic/apyrimidinic-site endonucleases, with the sites of strand scission by both agents corresponding to the location of the mismatch. These findings indicate that MutY is a DNA glycosylase that hydrolyzes the glycosyl bond linking the mis-paired adenine to deoxyribose. MutY, a 5'-apurinic/apyrimidinic-site endonuclease, DNA polymerase I, and DNA ligase are sufficient to reconstitute MutY-dependent G-A to G.C repair in vitro. |
| Links | |
| Keywords |
Adenine; Base Composition; DNA Glycosylases; DNA Repair; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Guanine; N-Glycosyl Hydrolases/genetics; N-Glycosyl Hydrolases/isolation & purification; N-Glycosyl Hydrolases/metabolism |
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