PMID:18390656
| Citation |
Uehara, T and Park, JT (2008) Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation. J. Bacteriol. 190:3914-22 |
|---|---|
| Abstract |
We have found a striking difference between the modes of action of amdinocillin (mecillinam) and compound A22, both of which inhibit cell elongation. This was made possible by employment of a new method using an Escherichia coli peptidoglycan (PG)-recycling mutant, lacking ampD, to analyze PG degradation during cell elongation and septation. Using this method, we have found that A22, which is known to prevent MreB function, strongly inhibited PG synthesis during elongation. In contrast, treatment of elongating cells with amdinocillin, which inhibits penicillin-binding protein 2 (PBP2), allowed PG glycan synthesis to proceed at a nearly normal rate with concomitant rapid degradation of the new glycan strands. By treating cells with A22 to inhibit sidewall synthesis, the method could also be applied to study septum synthesis. To our surprise, over 30% of newly synthesized septal PG was degraded during septation. Thus, excess PG sufficient to form at least one additional pole was being synthesized and rapidly degraded during septation. We propose that during cell division, rapid removal of the excess PG serves to separate the new poles of the daughter cells. We have also employed this new method to demonstrate that PBP2 and RodA are required for the synthesis of glycan strands during elongation and that the periplasmic amidases that aid in cell separation are minor players, cleaving only one-sixth of the PG that is turned over by the lytic transglycosylases. |
| Links |
PubMed PMC2395050 Online version:10.1128/JB.00207-08 |
| Keywords |
Amdinocillin/pharmacology; Amidohydrolases/metabolism; Anti-Bacterial Agents/pharmacology; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Wall/metabolism; Escherichia coli/drug effects; Escherichia coli/growth & development; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mutation; N-Acetylmuramoyl-L-alanine Amidase/genetics; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Penicillin-Binding Proteins/genetics; Penicillin-Binding Proteins/metabolism; Peptidoglycan/metabolism; Periplasm/enzymology; Thiourea/analogs & derivatives; Thiourea/pharmacology |
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Useful Materials and Methods
This paper used 2 antibiotics to inhibit cell elongation: A22 and amdinocillin. A22 disturbs the subcellular localization of MreB while amdinocillin specifically inhibits PBP2.
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