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PMID: 17993535 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli.

Journal of bacteriology ·Vol. 190 ·No. 5 ·2008-03-00 ·Pages 1792-811

Bendezú FO, de Boer PA

Abstract

Maintenance of rod shape in Escherichia coli requires the shape proteins MreB, MreC, MreD, MrdA (PBP2), and MrdB (RodA). How loss of the Mre proteins affects E. coli viability has been unclear. We generated Mre and Mrd depletion strains under conditions that minimize selective pressure for undefined suppressors and found their phenotypes to be very similar. Cells lacking one or more of the five proteins were fully viable and propagated as small spheres under conditions of slow mass increase but formed large nondividing spheroids with noncanonical FtsZ assembly patterns at higher mass doubling rates. Extra FtsZ was sufficient to suppress lethality in each case, allowing cells to propagate as small spheres under any condition. The failure of each unsuppressed mutant to divide under nonpermissive conditions correlated with the presence of elaborate intracytoplasmic membrane-bound compartments, including vesicles/vacuoles and more-complex systems. Many, if not all, of these compartments formed by FtsZ-independent involution of the cytoplasmic membrane (CM) rather than de novo. Remarkably, while some of the compartments were still continuous with the CM and the periplasm, many were topologically separate, indicating they had been released into the cytoplasm by an endocytic-like membrane fission event. Notably, cells failed to adjust the rate of phospholipid synthesis to their new surface requirements upon depletion of MreBCD, providing a rationale for the "excess" membrane in the resulting spheroids. Both FtsZ and MinD readily assembled on intracytoplasmic membrane surfaces, and we propose that this contributes significantly to the lethal division block seen in all shape mutants under nonpermissive conditions.

MeSH Terms
Adenosine Triphosphatases/genetics,metabolism Bacterial Proteins/genetics,metabolism Cell Membrane/metabolism Dimerization Endocytosis/genetics Escherichia coli/cytology,genetics,metabolism Escherichia coli Proteins/chemistry,genetics,metabolism Membrane Proteins/genetics,metabolism Microbial Viability/genetics Microscopy, Confocal Models, Genetic Mutation Phospholipids/metabolism Trans-Activators/genetics,metabolism
Chemicals
Bacterial Proteins Escherichia coli Proteins FtsZ84 protein, E coli Membrane Proteins MreC protein, Bacteria MreD protein, E coli Phospholipids Trans-Activators sdiA protein, E coli mrdB protein, E coli MreB protein, E coli Adenosine Triphosphatases MinD protein, E coli
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bendezú Felipe O
Case Western Reserve University, School of Medicine, Department of Molecular Biology and Microbiology, Cleveland, OH 44106, USA.
de Boer Piet A J
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
1098-5530
Published
2008-03-00
Epub
2007-00-09
Pages
1792-811
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC2258658
Subset
IM
Grants
NIGMS NIH HHS · T32GM08056 · United States
NCI NIH HHS · P30 CA043703 · United States
NIGMS NIH HHS · T32 GM008056 · United States
NCI NIH HHS · P30 CA43703 · United States
NIGMS NIH HHS · GM57059 · United States
NIGMS NIH HHS · R01 GM057059-10 · United States
NIGMS NIH HHS · R01 GM057059 · United States
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