The MutS C terminus is essential for mismatch repair activity in vivo

J Bacteriol. 2005 Sep;187(18):6577-9. doi: 10.1128/JB.187.18.6577-6579.2005.

Abstract

An Escherichia coli K-12 strain was constructed with a chromosomal deletion (mutSdelta800) in the mutS gene that produced the removal of the C-terminal 53 amino acids which are not present in the MutS crystal structure. This strain has a MutS null phenotype for mutation avoidance, anti-recombination, and sensitivity to cytotoxic agents in a dam mutant background.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Base Pair Mismatch
  • DNA Repair / physiology*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli / genetics*
  • Escherichia coli / physiology
  • Escherichia coli Proteins*
  • MutS DNA Mismatch-Binding Protein
  • Mutation*

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Adenosine Triphosphatases
  • MutS DNA Mismatch-Binding Protein
  • MutS protein, E coli