From the regulation of peptidoglycan synthesis to bacterial growth and morphology

Typas, Athanasios; Banzhaf, Manuel; Gross, Carol A.; Vollmer, Waldemar

doi:10.1038/nrmicro2677

Cited by 1,098 publications

(1,311 citation statements)

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“…There are additional, fascinating questions associated with the intersection of mechanics and bacterial growth, that we shall not discuss here, such as the forces exerted by the Z-ring in the bacterial division process (Egan and Vollmer 2013;Li et al 2013;Piro et al 2013;Sun and Jiang 2011), the role of crescentin in shaping curved cells (Cabeen et al 2009), and the growth of curved and helical bacteria (Sycuro et al 2010;Typas et al 2011), to name but a few.…”

Section: Introductionmentioning

confidence: 99%

Getting into shape: How do rod-like bacteria control their geometry?

Amir¹,

Teeffelen²

2014

Syst Synth Biol

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Rod-like bacteria maintain their cylindrical shapes with remarkable precision during growth. However, they are also capable to adapt their shapes to external forces and constraints, for example by growing into narrow or curved confinements. Despite being one of the simplest morphologies, we are still far from a full understanding of how shape is robustly regulated, and how bacteria obtain their near-perfect cylindrical shapes with excellent precision. However, recent experimental and theoretical findings suggest that cell-wall geometry and mechanical stress play important roles in regulating cell shape in rod-like bacteria. We review our current understanding of the cell wall architecture and the growth dynamics, and discuss possible candidates for regulatory cues of shape regulation in the absence or presence of external constraints. Finally, we suggest further future experimental and theoretical directions which may help to shed light on this fundamental problem.

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Section: Introductionmentioning

confidence: 99%

Getting into shape: How do rod-like bacteria control their geometry?

Amir¹,

Teeffelen²

2014

Syst Synth Biol

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“…B acterial cell shape is structurally determined by a rigid peptidoglycan (PG) cell wall built outside of the cytoplasmic membrane by a series of cell wall assembly enzymes (1). In many rod-shaped species these enzymes are coordinated by the actinlike protein, MreB, though the mechanism coupling this cytoplasmic protein to the extracellular cell wall enzymes and the specific functions executed by MreB have remained largely mysterious.…”

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confidence: 99%

RodZ links MreB to cell wall synthesis to mediate MreB rotation and robust morphogenesis

Morgenstein

Bratton

Nguyen

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

113

166

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The rod shape of most bacteria requires the actin homolog, MreB. Whereas MreB was initially thought to statically define rod shape, recent studies found that MreB dynamically rotates around the cell circumference dependent on cell wall synthesis. However, the mechanism by which cytoplasmic MreB is linked to extracytoplasmic cell wall synthesis and the function of this linkage for morphogenesis has remained unclear. Here we demonstrate that the transmembrane protein RodZ mediates MreB rotation by directly or indirectly coupling MreB to cell wall synthesis enzymes. Furthermore, we map the RodZ domains that link MreB to cell wall synthesis and identify mreB mutants that suppress the shape defect of ΔrodZ without restoring rotation, uncoupling rotation from rod-like growth. Surprisingly, MreB rotation is dispensable for rodlike shape determination under standard laboratory conditions but is required for the robustness of rod shape and growth under conditions of cell wall stress.bacterial cytoskeleton | bacterial cell shape | cell growth | cytoskeleton dynamics | robust rod shape B acterial cell shape is structurally determined by a rigid peptidoglycan (PG) cell wall built outside of the cytoplasmic membrane by a series of cell wall assembly enzymes (1). In many rod-shaped species these enzymes are coordinated by the actinlike protein, MreB, though the mechanism coupling this cytoplasmic protein to the extracellular cell wall enzymes and the specific functions executed by MreB have remained largely mysterious. Polymeric MreB is necessary to maintain rod-shaped cells, as inhibition of MreB polymerization or deletion of mreB cause cells to lose their rod shape. Initially, MreB was thought to form long helical structures that statically define rod shape (2, 3). Later, improved fluorescent fusion proteins and imaging methods revealed that MreB forms short polymers that dynamically rotate around the cell circumference (4-7).This circumferential rotation requires cell wall synthesis and is conserved across both Gram-negative and Gram-positive species (5-7), leading multiple groups to conclude that rotation promotes rod-shape formation. However, experimentally testing this hypothesis has proven difficult because all previous attempts to disrupt rotation have either led to cell death or massive cell shape changes, making it impossible to isolate the specific function of MreB rotation (5, 6). Furthermore, it remained difficult to explain the mechanistic link between cell wall growth and MreB rotation because of their separation in space by the cytoplasmic membrane. Here, we address both the coupling of MreB to cell wall synthesis and the function of MreB rotation. Results and DiscussionRodZ Rotates Similarly to MreB. We initially set out to identify proteins necessary for MreB rotation. In Escherichia coli, multiple proteins have been suggested to interact with MreB, including the penicillin binding protein (PBP) cell wall synthesis enzymes and RodZ, an integral membrane protein that directly binds MreB (8-11). PBP2 inhibitor...

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“…Average polymer length (subunits) Total FtsZ concentration (µM) Number of FtsZ molecules Contraction parameter (i 2 av Z N ) 1 2 3 The cell is conceptually divided into three compartments: the cell caps (1), the midcell (2), and the midcell membrane (3). FtsZ moves between the cell caps and the midcell regions by di usion.…”

Section: Figure1mentioning

confidence: 99%

“…For recent reviews see Typas et al, Egan and Vollmer, and den Blaauwen. [3][4][5] Despite extensive work since the discovery in 1991 that FtsZ is the major component of the contractile ring, 6 the mechanism driving the assembly and contraction of the Z-ring as well as the link between protein function and cellular phenotype remain poorly understood. Translation of the activity of FtsZ measured in vitro to its function in vivo is critical to further our understanding of cytokinesis.…”

Section: Introductionmentioning

confidence: 99%

Biological Insights from a Simulation Model of the Critical FtsZ Accumulation Required for Prokaryotic Cell Division

Dow

Berg²,

Roper

et al. 2015

Biochemistry

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Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work of researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-forprofit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. Publisher's statement:This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/abs/10.1021/acs.biochem.5b00261The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP url' above for details on accessing the published version and note that access may require a subscription. FtsZ in vitro as well as on in vivo parameters, is used to integrate critical processes in cell division. According to the model, the cell's ability to divide depends on a "contraction parameter" (χ) that links the force of contraction to the dynamics of FtsZ. This parameter accurately predicts the outcome of division. Evaluating the GTP binding strength, the FtsZ polymerization rate, and the intrinsic GTP hydrolysis/dissociation activity, we find that inhibition of GTP-FtsZ binding is an inefficient anti-bacterial target. Furthermore, simulations indicate that the temperature sensitivity of the ftsZ84 mutation arises from the 2 conversion of FtsZ to a dual-specificity NTPase. Finally, the sensitivity to temperature of the rate of ATP hydrolysis, over the critical temperature range, leads us to conclude that the ftsZ84 mutation affects the turnover rate of the Z-ring much less strongly than previously reported.

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From the regulation of peptidoglycan synthesis to bacterial growth and morphology

Cited by 1,098 publications

References 138 publications

Getting into shape: How do rod-like bacteria control their geometry?

Getting into shape: How do rod-like bacteria control their geometry?

RodZ links MreB to cell wall synthesis to mediate MreB rotation and robust morphogenesis

Biological Insights from a Simulation Model of the Critical FtsZ Accumulation Required for Prokaryotic Cell Division

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