Alterations of murein structure and of penicillin-binding proteins in minicells from Escherichia coli

Microbiology. 1994 Jan;140 ( Pt 1):79-87. doi: 10.1099/13500872-140-1-79.

Abstract

Minicells, as compared with a whole cell preparation of a minA/B mutant of Escherichia coli, showed a number of changes in the structure of the murein sacculus. Minicell murein was enriched in LD-A2pm-A2pm crossbridges by about 66% and reduced in the amount of L-Ala-D-Glu dipeptide moieties by about 55%. In addition, the length distribution of the glycan strands in the murein was shifted to shorter lengths. In particular, the relative amount of the shortest possible strand, the size of a disaccharide, was more than doubled. Minicells were also found to have an altered penicillin-binding protein (PBP) pattern. Whereas PBP4 and PBP6 were greatly diminished, PBP8 was significantly increased. We consider it unlikely that the sort of changes observed in murein structure reflect the fact that minicells are composed of two hemispherical polar caps.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Carbohydrate Sequence
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Cell Division
  • Escherichia coli / chemistry*
  • Escherichia coli / cytology
  • Escherichia coli / genetics
  • Hexosyltransferases*
  • Molecular Sequence Data
  • Molecular Structure
  • Muramoylpentapeptide Carboxypeptidase / chemistry*
  • Muramoylpentapeptide Carboxypeptidase / genetics
  • Mutation
  • Penicillin-Binding Proteins
  • Peptidoglycan / chemistry*
  • Peptidoglycan / genetics
  • Peptidyl Transferases*
  • Polysaccharides / chemistry

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • Peptidoglycan
  • Polysaccharides
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase