Affiliation:
1. Centro de Biologı́a Molecular “Severo Ochoa,” Consejo Superior de Investigaciones Cientı́ficas-Universidad Autónoma de Madrid, Campus de Cantoblanco, 28049 Madrid, Spain1;
2. Institute of Cell and Molecular Biology, The University of Edinburgh, Edinburgh EH9 3JR, Scotland2; and
3. Max-Planck Institut für Entwitcklungsbiologie, D-7400 Tübingen, Germany3
Abstract
ABSTRACT
The pattern of peptidoglycan (murein) segregation in cells of
Escherichia coli
with impaired activity of the morphogenetic proteins penicillin-binding protein 2 and RodA has been investigated by the
d
-cysteine–biotin immunolabeling technique (M. A. de Pedro, J. C. Quintela, J.-V. Höltje, and H. Schwarz, J. Bacteriol. 179:2823–2834, 1997). Inactivation of these proteins either by amdinocillin treatment or by mutations in the corresponding genes,
pbpA
and
rodA
, respectively, leads to the generation of round, osmotically stable cells. In normal rod-shaped cells, new murein precursors are incorporated all over the lateral wall in a diffuse manner, being mixed up homogeneously with preexisting material, except during septation, when strictly localized murein synthesis occurs. In contrast, in rounded cells, incorporation of new precursors is apparently a zonal process, localized at positions at which division had previously taken place. Consequently, there is no mixing of new and old murein. Old murein is preserved for long periods of time in large, well-defined areas. We propose that the observed patterns are the result of a failure to switch off septal murein synthesis at the end of septation events. Furthermore, the segregation results confirm that round cells of
rodA
mutants do divide in alternate, perpendicular planes as previously proposed (K. J. Begg and W. D. Donachie, J. Bacteriol. 180:2564–2567, 1998).
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
100 articles.
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