ArticleProceedings of the National Academy of Sciences of the United States of America2005
Two independent spiral structures control cell shape in Caulobacter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed.
- DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus.Nature communications · 2023Article
- Article
- The crystal structure of MreC provides insights into polymer formation.FEBS open bio · 2022Article
- Self-association of MreC as a regulatory signal in bacterial cell wall elongation.Nature communications · 2021Article
- Identification of potential regulatory domains within the MreC and MreD components of the cell elongation machinery.Journal of bacteriology · 2021Article
- The Inorganic Nutrient Regime and themSphere · 2020Article
- Penicillin-binding proteins regulate multiple steps in the polarized cell division process of Chlamydia.Scientific reports · 2020Article
- Article
- Chemical synthesis rewriting of a bacterial genome to achieve design flexibility and biological functionality.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A specialized MreB-dependent cell wall biosynthetic complex mediates the formation of stalk-specific peptidoglycan in Caulobacter crescentus.PLoS genetics · 2019Article
- Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex.Nature communications · 2017Article
- Evolution of polymer formation within the actin superfamily.Molecular biology of the cell · 2017Review
- Shapeshifting to Survive: Shape Determination and Regulation in Caulobacter crescentus.Trends in microbiology · 2017Review
- Coarse-grained simulations of bacterial cell wall growth reveal that local coordination alone can be sufficient to maintain rod shape.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- The effect of inhibition of host MreB on the infection of thermophilic phage GVE2 in high temperature environment.Scientific reports · 2014Article
- Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging.Nature reviews. Microbiology · 2014Review
- A mutation in the promoter region of zipA, a component of the divisome, suppresses the shape defect of RodZ-deficient cells.MicrobiologyOpen · 2013Article
- Multidimensional view of the bacterial cytoskeleton.Journal of bacteriology · 2013Review
- A potential role for differential contractility in early brain development and evolution.Biomechanics and modeling in mechanobiology · 2012Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
The actin homolog MreB contributes to bacterial cell shape. Here, we explore the role of the coexpressed MreC protein in Caulobacter and show that it forms a periplasmic spiral that is out of phase with the cytoplasmic MreB spiral. Both mreB and mreC are essential, and depletion of either protein results in a similar cell shape defect. MreB forms dynamic spirals in MreC-depleted cells, and MreC localizes helically in the presence of the MreB-inhibitor A22, indicating that each protein can form a spiral independently of the other. We show that the peptidoglycan transpeptidase Pbp2 also forms a helical pattern that partially colocalizes with MreC but not MreB. Perturbing either MreB (with A22) or MreC (with depletion) causes GFP-Pbp2 to mislocalize to the division plane, indicating that each is necessary but not sufficient to generate a helical Pbp2 pattern. We show that it is the division process that draws Pbp2 to midcell in the absence of MreB's regulation, because cells depleted of the tubulin homolog FtsZ maintain a helical Pbp2 localization in the presence of A22. By developing and employing a previously uncharacterized computational method for quantitating shape variance, we find that a FtsZ depletion can also partially rescue the A22-induced shape deformation. We conclude that MreB and MreC form spatially distinct and independently localized spirals and propose that MreB inhibits division plane localization of Pbp2, whereas MreC promotes lengthwise localization of Pbp2; together these two mechanism ensure a helical localization of Pbp2 and, thereby, the maintenance of proper cell morphology in Caulobacter.
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