RRC ID 29809
Author Ogura T, Bouloc P, Niki H, D'Ari R, Hiraga S, Jaffé A.
Title Penicillin-binding protein 2 is essential in wild-type Escherichia coli but not in lov or cya mutants.
Journal J. Bacteriol.
Abstract Penicillin-binding protein 2 (PBP2), target of the beta-lactam mecillinam, is required for rod morphology and cell wall elongation in Escherichia coli. A new temperature-sensitive PBP2 allele and an in vitro-constructed insertion deletion allele were shown to be lethal in wild-type strains, establishing that the activity of this protein is essential. Mutations in the lov or cya genes, conferring mecillinam resistance, compensated for the deleterious effect of the absence of PBP2. The resulting double mutants grew as spheres. In a cya mutant lacking PBP2, the restoration of a Cya+ phenotype by addition of cyclic AMP caused lethality and a block in cell division. These results show that in wild-type cells, PBP2 is essential for growth and division.
Volume 171(6)
Pages 3025-30
Published 1989-6
PMID 2656638
PMC PMC210010
MeSH Acyltransferases / physiology* Amdinocillin Bacterial Proteins* Carrier Proteins* Cell Division Cell Wall / ultrastructure Escherichia coli / genetics* Escherichia coli / ultrastructure Genes, Bacterial Genes, Lethal Genetic Complementation Test Hexosyltransferases / physiology* Multienzyme Complexes / physiology* Muramoylpentapeptide Carboxypeptidase* Mutation Penicillin Resistance Penicillin-Binding Proteins Peptidyl Transferases / physiology*
IF 3.219
Times Cited 63
Prokaryotes E. coli ME9620