RRC ID 29786
Author Spratt BG.
Title Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.
Journal Proc Natl Acad Sci U S A
Abstract The varied effects of beta-lactam antibiotics on cell division, cell elongation, and cell shape in E. coli are shown to be due to the presence of three essential penicillin binding proteins with distinct roles in these three processes. (A) Cell shape: beta-Lactams that specifically result in the production of ovoid cells bind to penicillin binding protein 2 (molecular weight 66,000). A mutant has been isolated that fails to bind beta-lactams to protein 2, and that grows as round cells. (B) Cell division: beta-Lactams that specifically inhibit cell division bind preferentially to penicillin binding protein 3 (molecular weight 60,000). A temperature-sensitive cell division mutant has been shown to have a thermolabile protein 3. (C) Cell elongation: One beta-lactam that preferentially inhibits cell elongation and causes cell lysis binds preferentially to binding protein 1 (molecular weight 91,000). Evidence is presented that penicillin bulge formation is due to the inhibition of proteins 2 and 3 in the absence of inhibition of protein 1.
Volume 72(8)
Pages 2999-3003
Published 1975-8-1
DOI 10.1073/pnas.72.8.2999
PMID 1103132
PMC PMC432906
MeSH Ampicillin / metabolism Bacterial Proteins / metabolism* Binding Sites Cell Division / drug effects Cephaloridine / metabolism Escherichia coli / physiology* Kinetics Penicillin G / metabolism Penicillins / metabolism* Penicillins / pharmacology Protein Binding Receptors, Drug*
IF 9.412
Resource
Prokaryotes E. coli JE5780