The frequency of MMS-induced, umuDC-dependent, mutations declines during starvation in Escherichia coli

Mol Gen Genet. 1994 Nov 15;245(4):486-92. doi: 10.1007/BF00302261.

Abstract

It has been found that the level of methyl methanesulfonate (MMS)-induced mutation in Escherichia coli is dependent on the level of UmuD(D')C proteins. The frequency of argE(ochre)-->Arg+ mutations (which occur predominantly by AT-->TA transversions) and RifS-->RifR mutations is much higher when UmuDC or UmuD'C are overproduced in the cell. When MMS-treated bacteria were starved for progressively longer times and hence the expression of mutations delayed, the level of mutations observed progressively declined. This same treatment had no effect on the degree of SOS induction. Examination of plasmid DNAs, isolated from MMS-treated cells, for their sensitivity to the specific endonucleases Fpg and Nth revealed that MMS causes formation of abasic sites, which are repaired during cell starvation. It is assumed that, in non-dividing cells, apurinic sites are mostly repaired by RecA-mediated recombinational repair. This pathway, which is error-free, is compared with the processing pathway in metabolically active cells, where translesion synthesis by the UmuD'2C-RecA-DNA polymerase III holoenzyme complex occurs; this latter pathway is error-prone.

MeSH terms

  • Apurinic Acid / metabolism
  • Bacterial Proteins / metabolism
  • Cell Division
  • DNA Damage
  • DNA Repair / physiology*
  • DNA, Bacterial / metabolism
  • DNA-Directed DNA Polymerase
  • Escherichia coli / drug effects*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Methyl Methanesulfonate / toxicity
  • Mutagenesis
  • Point Mutation
  • Rec A Recombinases / metabolism*

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Escherichia coli Proteins
  • Apurinic Acid
  • UmuC protein, E coli
  • Methyl Methanesulfonate
  • Rec A Recombinases
  • DNA-Directed DNA Polymerase
  • UmuD protein, E coli