ArticleMolecular microbiology2010
A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 64 citations in OpenAlex.
- A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Outer Membrane Vesicles fromACS nano · 2025Article
- Article
- An outer membrane porin-lipoprotein complex modulates elongasome movement to establish cell curvature in Rhodospirillum rubrum.Nature communications · 2024Article
- Cell cycle dependent coordination of surface layer biogenesis in Caulobacter crescentus.Nature communications · 2024Article
- A dynamic bactofilin cytoskeleton cooperates with an M23 endopeptidase to control bacterial morphogenesis.eLife · 2024Article
- Influence of the Heme Nitric Oxide/Oxygen Binding Protein (H-NOX) on Cell Cycle Regulation in Caulobacter crescentus.Molecular & cellular proteomics : MCP · 2023Article
- DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus.Nature communications · 2023Article
- A LytM-Domain Factor, ActS, Functions in Two Distinctive Peptidoglycan Hydrolytic Pathways inFrontiers in microbiology · 2022Article
- Characterization of antibacterial activity of a N-acetylmuramoyl-L-alanine amidase produced by Latilactobacillus sakei isolated from salami.World journal of microbiology & biotechnology · 2021Article
- Diversification of LytM Protein Functions in Polar Elongation and Cell Division ofFrontiers in microbiology · 2021Article
- Sugar-Phosphate Metabolism Regulates Stationary-Phase Entry and Stalk Elongation in Caulobacter crescentus.Journal of bacteriology · 2020Article
- A specialized MreB-dependent cell wall biosynthetic complex mediates the formation of stalk-specific peptidoglycan in Caulobacter crescentus.PLoS genetics · 2019Article
- Fluorescent Proteins, Promoters, and Selectable Markers for Applications in the Lyme Disease Spirochete Borrelia burgdorferi.Applied and environmental microbiology · 2018Article
- Seven-transmembrane receptor protein RgsP and cell wall-binding protein RgsM promote unipolar growth in Rhizobiales.PLoS genetics · 2018Article
- YtfB, an OapA Domain-Containing Protein, Is a New Cell Division Protein in Escherichia coli.Journal of bacteriology · 2018Article
- Constriction Rate Modulation Can Drive Cell Size Control and Homeostasis in C. crescentus.iScience · 2018Article
- Amidase activity is essential for medial localization of AmiC in Caulobacter crescentus.Current genetics · 2018Article
- FtsEX-mediated regulation of the final stages of cell division reveals morphogenetic plasticity in Caulobacter crescentus.PLoS genetics · 2017Article
- Shapeshifting to Survive: Shape Determination and Regulation in Caulobacter crescentus.Trends in microbiology · 2017Review
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4 authors at 3 institutions in 3 countries.
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Abstract
During division of Gram-negative bacteria, invagination of the cytoplasmic membrane and inward growth of the peptidoglycan (PG) are followed by the cleavage of connective septal PG to allow cell separation. This PG splitting process requires temporal and spatial regulation of cell wall hydrolases. In Escherichia coli, LytM factors play an important role in PG splitting. Here we identify and characterize a member of this family (DipM) in Caulobacter crescentus. Unlike its E. coli counterparts, DipM is essential for viability under fast-growth conditions. Under slow-growth conditions, the DeltadipM mutant displays severe defects in cell division and FtsZ constriction. Consistent with its function in division, DipM colocalizes with the FtsZ ring during the cell cycle. Mutagenesis suggests that the LytM domain of DipM is essential for protein function, despite being non-canonical. DipM also carries two tandems of the PG-binding LysM domain that are sufficient for FtsZ ring localization. Localization and fluorescence recovery after photobleaching microscopy experiments suggest that DipM localization is mediated, at least in part, by the ability of the LysM tandems to distinguish septal, multilayered PG from non-septal, monolayered PG.
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