Chemical adaptation of M. luteus induces repair functions for O-alkylated DNA pyrimidines

Nucleic Acids Res. 1985 Oct 11;13(19):7153-66. doi: 10.1093/nar/13.19.7153.

Abstract

A partially purified extract prepared from adapted M. luteus cells contains repair functions for oxygen methylated pyrimidine residues present in alkylated DNA. The removal of O2-MeT is mediated by a DNA glycosylase enzyme whereas disappearance of O4-MeT is effected by a methyltransferase in a manner similar to the in situ repair of O6-MeG. O4-MeT methyltransferase enzyme is unusually heat resistant. Synthesis of these repair proteins, which are distinctly different from the previously known inducible 3-MeA DNA glycosylase and O6-MeG methyltransferase activities, forms a part of the adaptive response.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • DNA Glycosylases
  • DNA Repair*
  • Hot Temperature
  • Methylation
  • Methylnitronitrosoguanidine / toxicity
  • Methyltransferases / metabolism*
  • Micrococcus / genetics*
  • N-Glycosyl Hydrolases / metabolism
  • Pyrimidine Nucleotides / metabolism*

Substances

  • Pyrimidine Nucleotides
  • Methylnitronitrosoguanidine
  • Methyltransferases
  • DNA Glycosylases
  • N-Glycosyl Hydrolases