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Involvement of N ‐acetylmuramyl‐ l ‐alanine amidases in cell separation and antibiotic‐induced autolysis of Escherichia coli

Involvement of N ‐acetylmuramyl‐ l ‐alanine amidases in cell separation and antibiotic‐induced... N‐acetylmuramyl‐l‐alanine amidases are widely distributed among bacteria. However, in Escherichia coli, only one periplasmic amidase has been described until now, which is suggested to play a role in murein recycling. Here, we report that three amidases, named AmiA, B and C, exist in E. coli and that they are involved in splitting of the murein septum during cell division. Moreover, the amidases were shown to act as powerful autolytic enzymes in the presence of antibiotics. Deletion mutants in amiA, B and C were growing in long chains of unseparated cells and displayed a tolerant response to the normally lytic combination of aztreonam and bulgecin. Isolated murein sacculi of these chain‐forming mutants showed rings of thickened murein at the site of blocked septation. In vitro, these murein ring structures were digested more slowly by muramidases than the surrounding murein. In contrast, when treated with the amidase AmiC or the endopeptidase MepA, the rings disappeared, and gaps developed at these sites in the murein sacculi. These results are taken as evidence that highly stressed murein cross‐bridges are concentrated at the site of blocked cell division, which, when cleaved, result in cracking of the sacculus at this site. As amidase deletion mutants accumulate trimeric and tetrameric cross‐links in their murein, it is suggested that these structures mark the division site before cleavage of the septum. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular Microbiology Wiley

Involvement of N ‐acetylmuramyl‐ l ‐alanine amidases in cell separation and antibiotic‐induced autolysis of Escherichia coli

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References (56)

Publisher
Wiley
Copyright
Copyright © 2001 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0950-382X
eISSN
1365-2958
DOI
10.1046/j.1365-2958.2001.02499.x
Publisher site
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Abstract

N‐acetylmuramyl‐l‐alanine amidases are widely distributed among bacteria. However, in Escherichia coli, only one periplasmic amidase has been described until now, which is suggested to play a role in murein recycling. Here, we report that three amidases, named AmiA, B and C, exist in E. coli and that they are involved in splitting of the murein septum during cell division. Moreover, the amidases were shown to act as powerful autolytic enzymes in the presence of antibiotics. Deletion mutants in amiA, B and C were growing in long chains of unseparated cells and displayed a tolerant response to the normally lytic combination of aztreonam and bulgecin. Isolated murein sacculi of these chain‐forming mutants showed rings of thickened murein at the site of blocked septation. In vitro, these murein ring structures were digested more slowly by muramidases than the surrounding murein. In contrast, when treated with the amidase AmiC or the endopeptidase MepA, the rings disappeared, and gaps developed at these sites in the murein sacculi. These results are taken as evidence that highly stressed murein cross‐bridges are concentrated at the site of blocked cell division, which, when cleaved, result in cracking of the sacculus at this site. As amidase deletion mutants accumulate trimeric and tetrameric cross‐links in their murein, it is suggested that these structures mark the division site before cleavage of the septum.

Journal

Molecular Microbiology – Wiley

Published: Jul 1, 2001

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