Behavior of penicillin-binding proteins in Escherichia coli upon heat and detergent treatments and partial purification of penicillin-binding proteins 1A and 1B.

Journal of bacteriology ·Vol. 138 ·No. 3 ·1979-06-00 ·Pages 1029-32

Matsuzawa H, Datta P, Matsuhashi M

Abstract

Penicillin-binding proteins differ greatly in heat sensitivity and sensitivity to detergents. The partial purification of penicillin-binding 1A and 1B proteins from Escherichia coli is described.

MeSH Terms

Bacterial Proteins/isolation & purification,metabolism Carrier Proteins/isolation & purification,metabolism Cell Membrane/metabolism Escherichia coli/analysis,drug effects,metabolism Hot Temperature Penicillin G/metabolism Solubility Surface-Active Agents/pharmacology

Chemicals

Bacterial Proteins Carrier Proteins Surface-Active Agents Penicillin G

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Matsuzawa H

Datta P

Matsuhashi M

References (15)

15 references, click to expand

On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins.
Proc Natl Acad Sci U S A. 1978 Feb;75(2):664-8 PMID: 345275
Isolation of a mutant of Escherichia coli lacking penicillin-sensitive D-alanine carboxypeptidase IA.
Proc Natl Acad Sci U S A. 1978 Jun;75(6):2631-5 PMID: 351612
Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity.
J Bacteriol. 1979 Jan;137(1):644-7 PMID: 368033
Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12.
Proc Natl Acad Sci U S A. 1977 Jul;74(7):2980-4 PMID: 331323
Escherichia coli resistance to beta-lactam antibiotics through a decrease in the affinity of a target for lethality.
Nature. 1978 Aug 17;274(5672):713-5 PMID: 209344
Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro.
Proc Natl Acad Sci U S A. 1977 Dec;74(12):5472-6 PMID: 341159
Temperature-sensitive cell division mutants of Escherichia coli with thermolabile penicillin-binding proteins.
J Bacteriol. 1977 Jul;131(1):293-305 PMID: 326764
Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable.
FEBS Lett. 1977 Jul 15;79(2):374-8 PMID: 330236
Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.
Proc Natl Acad Sci U S A. 1977 Jul;74(7):2976-9 PMID: 331322
Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli.
J Biol Chem. 1976 Jan 25;251(2):414-23 PMID: 1391
Penicillin-resistant temperature-sensitive mutants of Escherichia coli which synthesize hypo- or hyper-cross-linked peptidoglycan.
J Bacteriol. 1974 Feb;117(2):568-77 PMID: 4590477
Biosynthesis of the peptidoglycan of bacterial cell walls. 8. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of Escherichia coli.
J Biol Chem. 1968 Jun 10;243(11):3180-92 PMID: 4871205
Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions.
Proc Natl Acad Sci U S A. 1966 Mar;55(3):656-63 PMID: 5329013
Penicillin-binding proteins and cell shape in E. coli.
Nature. 1975 Apr 10;254(5500):516-7 PMID: 1091862
Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.
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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.138.3.1029-1032.1979

Published

1979-06-00

Pages

1029-32

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC218137

Subset

External Links

PubMed source DOI: 10.1128/jb.138.3.1029-1032.1979 PMC Full Text View journal details

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Behavior of penicillin-binding proteins in Escherichia coli upon heat and detergent treatments and partial purification of penicillin-binding proteins 1A and 1B.

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