ArticleMolecular microbiology2010
DipM links peptidoglycan remodelling to outer membrane organization in Caulobacter.
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 43 papers.
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43 citing papers in PubMed, 71 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
- Article
- The Tol Pal system integrates maintenance of the three layered cell envelope.npj antimicrobials and resistance · 2024Review
- 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
- DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus.Nature communications · 2023Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Diversification of LytM Protein Functions in Polar Elongation and Cell Division ofFrontiers in microbiology · 2021Article
- An Essential Regulator of Bacterial Division Links FtsZ to Cell Wall Synthase Activation.Current biology : CB · 2019Article
- 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
- 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
- FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division.Molecular microbiology · 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
- The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division.Journal of bacteriology · 2017Review
- NlpD links cell wall remodeling and outer membrane invagination during cytokinesis in Escherichia coli.PLoS genetics · 2017Article
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5 authors at 2 institutions in 1 country.
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Abstract
Cell division in Gram-negative organisms requires coordinated invagination of the multilayered cell envelope such that each daughter receives an intact inner membrane, peptidoglycan (PG) layer and outer membrane (OM). Here, we identify DipM, a putative LytM endopeptidase in Caulobacter crescentus, and show that it plays a critical role in maintaining cell envelope architecture during growth and division. DipM localized to the division site in an FtsZ-dependent manner via its PG-binding LysM domains. Although not essential for viability, DeltadipM cells exhibited gross morphological defects, including cell widening and filamentation, indicating a role in cell shape maintenance and division that we show requires its LytM domain. Strikingly, cells lacking DipM also showed OM blebbing at the division site, at cell poles and along the cell body. Cryo electron tomography of sacculi isolated from cells depleted of DipM revealed marked thickening of the PG as compared to wild type, which we hypothesize leads to loss of trans-envelope contacts between components of the Tol-Pal complex. We conclude that DipM is required for normal envelope invagination during division and to maintain a sacculus of constant thickness that allows for maintenance of OM connections throughout the cell envelope.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.