Literature DB >> 8559061

Why does Escherichia coli recycle its cell wall peptides?

J T Park1.   

Abstract

This review discusses the phenomenon of recycling of cell wall peptides. It is a major, though non-essential, pathway of the cell and is required for induction of beta-lactamase. Consequently, the recycling pathway is viewed as a possible signalling vehicle, informing the cell of the condition of the murein sacculus, an essential structure existing outside the cell itself. As the study of this phenomenon is in its infancy, several speculations are offered for a possible regulatory function.

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Year:  1995        PMID: 8559061     DOI: 10.1111/j.1365-2958.1995.mmi_17030421.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  48 in total

1.  Interference with murein turnover has no effect on growth but reduces beta-lactamase induction in Escherichia coli.

Authors:  A R Kraft; J Prabhu; A Ursinus; J V Höltje
Journal:  J Bacteriol       Date:  1999-12       Impact factor: 3.490

2.  ampR gene mutations that greatly increase class C beta-lactamase activity in Enterobacter cloacae.

Authors:  A Kuga; R Okamoto; M Inoue
Journal:  Antimicrob Agents Chemother       Date:  2000-03       Impact factor: 5.191

3.  Inactivation of the ampDE operon increases transcription of algD and affects morphology and encystment of Azotobacter vinelandii.

Authors:  C Núñez; S Moreno; L Cárdenas; G Soberón-Chávez; G Espín
Journal:  J Bacteriol       Date:  2000-09       Impact factor: 3.490

4.  Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2.

Authors:  M A de Pedro; W D Donachie; J V Höltje; H Schwarz
Journal:  J Bacteriol       Date:  2001-07       Impact factor: 3.490

5.  Tertiary structure of bacterial murein: the scaffold model.

Authors:  Boris A Dmitriev; Filip V Toukach; Klaus-Jürgen Schaper; Otto Holst; Ernst T Rietschel; Stefan Ehlers
Journal:  J Bacteriol       Date:  2003-06       Impact factor: 3.490

6.  AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli.

Authors:  T A Henderson; K D Young; S A Denome; P K Elf
Journal:  J Bacteriol       Date:  1997-10       Impact factor: 3.490

7.  Mutations affecting peptidoglycan acetylation in Neisseria gonorrhoeae and Neisseria meningitidis.

Authors:  Joseph P Dillard; Kathleen T Hackett
Journal:  Infect Immun       Date:  2005-09       Impact factor: 3.441

8.  AmpH, a bifunctional DD-endopeptidase and DD-carboxypeptidase of Escherichia coli.

Authors:  Silvia M González-Leiza; Miguel A de Pedro; Juan A Ayala
Journal:  J Bacteriol       Date:  2011-10-14       Impact factor: 3.490

9.  In vivo reversion to the wild-type beta-lactam resistance phenotype mediated by a plasmid carrying ampR and qnrA1 in Enterobacter cloacae.

Authors:  J J González-López; M Sabaté; S Lavilla; M N Larrosa; R M Bartolomé; G Prats
Journal:  Antimicrob Agents Chemother       Date:  2006-09       Impact factor: 5.191

10.  Membrane topology of the Escherichia coli AmpG permease required for recycling of cell wall anhydromuropeptides and AmpC beta-lactamase induction.

Authors:  Aicha Chahboune; Marc Decaffmeyer; Robert Brasseur; Bernard Joris
Journal:  Antimicrob Agents Chemother       Date:  2005-03       Impact factor: 5.191

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