A novel nucleotide excision repair for the conversion of an A/G mismatch to C/G base pair in E. coli.
A protein that binds specifically to A/G mismatches has been detected in E. coli by a gel electrophoresis DNA binding assay. A specific endonuclease is associated with the A/G mismatch-binding protein through two chromatographic steps. The endonuclease is specific for A/G-containing DNA fragments and has no cleavage activity on DNA containing the other seven possible mispairs or homoduplex DNA. The endonuclease simultaneously makes incisions at the first phosphodiester bond 3' to and the second phosphodiester bond 5' to the dA of the A/G mismatch. No incision site was detected on the other strand. These results are consistent with the unidirectional A to C conversion and short repair tract of a novel dam- and mutHLS-independent A/G repair pathway we have recently described. A nucleotide excision repair model is proposed for the conversion of an A/G mismatch to a C/G base pair.
D001426:Bacterial Proteins / Q000502:physiology*; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000502:physiology*; D004587:Electrophoresis, Agar Gel; D004706:Endodeoxyribonucleases / Q000502:physiology*; D004926:Escherichia coli / Q000235:genetics*; D006860:Hydrogen Bonding; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D004706:Endodeoxyribonucleases