Literature DB >> 1987637

Coordinate regulation of beta-lactamase induction and peptidoglycan composition by the amp operon.

E Tuomanen1, S Lindquist, S Sande, M Galleni, K Light, D Gage, S Normark.   

Abstract

The amp operon, which is located on the Escherichia coli chromosome, modulates the induction of plasmid-borne beta-lactamase genes by extracellular beta-lactam antibiotics. This suggests that the gene products AmpD and AmpE may function in the transduction of external signals. beta-Lactam antibiotics are analogs of cell wall components that can be released during cell wall morphogenesis of enterobacteria. The amp operon was studied to determine its importance in signal transduction during cell wall morphogenesis. The peptidoglycan compositions of amp mutants were determined by high-performance liquid chromatography and fast atom bombardment mass spectrometry. When a chromosomal or plasmid-borne copy of ampD was present, the amount of pentapeptide-containing muropeptides in the cell wall increased upon addition of the cell wall constituent diaminopimelic acid to the growth medium. These results suggest that beta-lactamase induction and modulation of the composition of the cell wall share elements of a regulatory circuit that involves AmpD. Escherichia coli requires AmpD to respond to extracellular signaling amino acids, such as diaminopimelic acid, and this signal transduction system may regulate peptidoglycan composition in response to cell wall turnover products.

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Year:  1991        PMID: 1987637     DOI: 10.1126/science.1987637

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  19 in total

Review 1.  Messenger functions of the bacterial cell wall-derived muropeptides.

Authors:  Marc A Boudreau; Jed F Fisher; Shahriar Mobashery
Journal:  Biochemistry       Date:  2012-03-27       Impact factor: 3.162

Review 2.  Origins and evolution of antibiotic resistance.

Authors:  Julian Davies; Dorothy Davies
Journal:  Microbiol Mol Biol Rev       Date:  2010-09       Impact factor: 11.056

3.  Model system to evaluate the effect of ampD mutations on AmpC-mediated beta-lactam resistance.

Authors:  Amber J Schmidtke; Nancy D Hanson
Journal:  Antimicrob Agents Chemother       Date:  2006-06       Impact factor: 5.191

4.  Induction of a class I beta-lactamase from Citrobacter freundii in Escherichia coli requires active ftsZ but not ftsA or ftsQ products.

Authors:  A C Ottolenghi; J A Ayala
Journal:  Antimicrob Agents Chemother       Date:  1991-11       Impact factor: 5.191

5.  Deletion of an additional domain located between SXXK and SXN active-site fingerprints in penicillin-binding protein 4 from Escherichia coli.

Authors:  H Mottl; P Nieland; G de Kort; J J Wierenga; W Keck
Journal:  J Bacteriol       Date:  1992-05       Impact factor: 3.490

Review 6.  The sentinel role of peptidoglycan recycling in the β-lactam resistance of the Gram-negative Enterobacteriaceae and Pseudomonas aeruginosa.

Authors:  Jed F Fisher; Shahriar Mobashery
Journal:  Bioorg Chem       Date:  2014-06-04       Impact factor: 5.275

Review 7.  Antibiotic resistance and its cost: is it possible to reverse resistance?

Authors:  Dan I Andersson; Diarmaid Hughes
Journal:  Nat Rev Microbiol       Date:  2010-03-08       Impact factor: 60.633

8.  The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide.

Authors:  H Dietz; D Pfeifle; B Wiedemann
Journal:  Antimicrob Agents Chemother       Date:  1997-10       Impact factor: 5.191

9.  Identification of ZipA, a signal recognition particle-dependent protein from Neisseria gonorrhoeae.

Authors:  Ying Du; Cindy Grove Arvidson
Journal:  J Bacteriol       Date:  2003-04       Impact factor: 3.490

10.  The Pseudomonas cepacia 249 chromosomal penicillinase is a member of the AmpC family of chromosomal beta-lactamases.

Authors:  R Proenca; W W Niu; G Cacalano; A Prince
Journal:  Antimicrob Agents Chemother       Date:  1993-04       Impact factor: 5.191

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