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Changes in peptidoglycan composition and penicillin-binding proteins in slowly growing Escherichia coli. 1987

E Tuomanen, and R Cozens
Rockefeller University, New York, New York 10021.

The composition of peptidoglycan of chemostat-grown cultures of Escherichia coli was investigated as a function of growth rate. As the generation time was lengthened from 0.8 to 13.8 h, there was a decrease in the major monomer (disaccharide tetrapeptide) and dimer (bis-disaccharide tetrapeptide), while disaccharide tripeptide moieties increased to greater than 50% of the total wall. The average chain length became much shorter; lipoprotein density tripled, and the number of unusual diaminopimelyl-diaminopimelic acid crossbridges increased fivefold. As cells grew more slowly, amounts of penicillin-binding proteins (PBPs) 1a-1b complex and 4 decreased, while amounts of PBPs 3 and the 5-6 complex increased. We propose that the chemical composition of E. coli cell walls changes with growth rate in a manner consistent with alterations in the activities of PBPs and cell shape.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D010457 Peptidoglycan A structural polymer of the bacterial cell envelope consisting of sugars and amino acids which is responsible for both shape determination and cellular integrity under osmotic stress in virtually all bacteria. Murein,Pseudomurein
D010458 Peptidyl Transferases Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases. Peptidyl Transferase,Peptidyl Translocase,Peptidyl Translocases,Peptidyltransferase,Transpeptidase,Transpeptidases,Peptidyltransferases,Transferase, Peptidyl,Transferases, Peptidyl,Translocase, Peptidyl,Translocases, Peptidyl
D002267 Muramoylpentapeptide Carboxypeptidase Enzyme which catalyzes the peptide cross-linking of nascent CELL WALL; PEPTIDOGLYCAN. Carboxypeptidase Transpeptidase,Carboxypeptidase, Muramoylpentapeptide,Transpeptidase, Carboxypeptidase
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D002851 Chromatography, High Pressure Liquid Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed. Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006602 Hexosyltransferases Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D046915 Penicillin-Binding Proteins Bacterial proteins that share the property of binding irreversibly to PENICILLINS and other ANTIBACTERIAL AGENTS derived from LACTAMS. The penicillin-binding proteins are primarily enzymes involved in CELL WALL biosynthesis including MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE; PEPTIDE SYNTHASES; TRANSPEPTIDASES; and HEXOSYLTRANSFERASES. Penicillin-Binding Protein,Penicillin-Binding Protein 1,Penicillin-Binding Protein 1A,Penicillin-Binding Protein 1b,Penicillin-Binding Protein 2,Penicillin-Binding Protein 2a,Penicillin-Binding Protein 2b,Penicillin-Binding Protein 3,Penicillin-Binding Protein 4,Penicillin-Binding Protein 5,Penicillin-Binding Protein 6,Penicillin-Binding Protein 7,Penicillin-Binding Protein-2a,Peptidoglycan Synthetase,Penicillin Binding Protein,Penicillin Binding Protein 1,Penicillin Binding Protein 1A,Penicillin Binding Protein 1b,Penicillin Binding Protein 2,Penicillin Binding Protein 2a,Penicillin Binding Protein 2b,Penicillin Binding Protein 3,Penicillin Binding Protein 4,Penicillin Binding Protein 5,Penicillin Binding Protein 6,Penicillin Binding Protein 7,Penicillin Binding Proteins,Protein 1A, Penicillin-Binding,Protein 1b, Penicillin-Binding,Proteins, Penicillin-Binding,Synthetase, Peptidoglycan

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