Identification of a new mutation in Escherichia coli that suppresses a pbpB (Ts) phenotype in the presence of penicillin-binding protein 1B

FEMS Microbiol Lett. 1991 Nov 1;68(1):7-13. doi: 10.1016/0378-1097(91)90386-o.

Abstract

Analysis of the functional role of penicillin-binding protein 1B (PBP1B) of Escherichia coli led us to find a new mutation able to suppress thermosensitive growth of the pbpB2158(Ts) mutant strain, which harbors a thermosensitive PBP3 protein only in the presence of a ponB+ background. The mutation, originally isolated in a strain with a high dosage of PBP1B, could also suppress the pbpB(Ts) phenotype when a single copy of the ponB gene was introduced. These results clearly give further support to the implication of PPB1B in the septation process in Escherichia coli.

MeSH terms

  • Bacterial Proteins*
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development
  • Escherichia coli Proteins*
  • Genotype
  • Hexosyltransferases*
  • Muramoylpentapeptide Carboxypeptidase / genetics*
  • Muramoylpentapeptide Carboxypeptidase / metabolism
  • Penicillin-Binding Proteins
  • Penicillins / metabolism*
  • Peptidoglycan Glycosyltransferase*
  • Peptidyl Transferases*
  • Phenotype
  • Serine-Type D-Ala-D-Ala Carboxypeptidase*
  • Suppression, Genetic*
  • Temperature

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • FtsI protein, E coli
  • Penicillin-Binding Proteins
  • Penicillins
  • Peptidyl Transferases
  • Hexosyltransferases
  • Peptidoglycan Glycosyltransferase
  • penicillin-binding protein 1B, E coli
  • Serine-Type D-Ala-D-Ala Carboxypeptidase
  • Muramoylpentapeptide Carboxypeptidase