ArticleJournal of bacteriology2012
Osmolality-dependent relocation of penicillin-binding protein PBP2 to the division site in Caulobacter crescentus.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Experimental Assessment of Iris Water Content and Sex Differences in Mature Rabbits.bioRxiv : the preprint server for biology · 2026Article
- An ancestral transmembrane transcription factor couples cell envelope regulation and the SOS response in Caulobacter crescentus.PLoS genetics · 2026Article
- Twin-arginine transport complex plays an essential role inMolecular biology of the cell · 2026Article
- Growth stage and interspecies interactions shape the cell biology and cell cycle characteristics of human gut bacteria Bacteroides thetaiotaomicron and Roseburia intestinalis.Communications biology · 2025Article
- Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025Article
- Complex interplay between gene deletions and the environment uncovers cellular roles for genes of unknown function inmSystems · 2025Article
- Phenotypic plasticity in cell elongation among closely related bacterial species.Nature communications · 2025Article
- Article
- Regulation of potassium uptake inJournal of bacteriology · 2024Article
- Distinct dynamics and proximity networks of hub proteins at the prey-invading cell pole in a predatory bacterium.Journal of bacteriology · 2024Article
- Cell division cycle fluctuation of Pal concentration in Escherichia coli.Access microbiology · 2024Article
- Cell cycle-dependent organization of a bacterial centromere through multi-layered regulation of the ParABS system.PLoS genetics · 2023Article
- A biologist's guide to planning and performing quantitative bioimaging experiments.PLoS biology · 2023Article
- Engineering osmolysis susceptibility in Cupriavidus necator and Escherichia coli for recovery of intracellular products.Microbial cell factories · 2023Article
- Comparative Modeling and Analysis of Extremophilic D-Ala-D-Ala Carboxypeptidases.Biomolecules · 2023Article
- A large screen identifies beta-lactam antibiotics which can be repurposed to target the syphilis agent.npj antimicrobials and resistance · 2023Article
- The two-component system ChvGI maintains cell envelope homeostasis in Caulobacter crescentus.PLoS genetics · 2022Article
- Article
- Early midcell localization of Escherichia coli PBP4 supports the function of peptidoglycan amidases.PLoS genetics · 2022Article
- Elongation at Midcell in Preparation of Cell Division Requires FtsZ, but Not MreB nor PBP2 inFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The synthesis of the peptidoglycan cell wall is carefully regulated in time and space. In nature, this essential process occurs in cells that live in fluctuating environments. Here we show that the spatial distributions of specific cell wall proteins in Caulobacter crescentus are sensitive to small external osmotic upshifts. The penicillin-binding protein PBP2, which is commonly branded as an essential cell elongation-specific transpeptidase, switches its localization from a dispersed, patchy pattern to an accumulation at the FtsZ ring location in response to osmotic upshifts as low as 40 mosmol/kg. This osmolality-dependent relocation to the division apparatus is initiated within less than a minute, while restoration to the patchy localization pattern is dependent on cell growth and takes 1 to 2 generations. Cell wall morphogenetic protein RodA and penicillin-binding protein PBP1a also change their spatial distribution by accumulating at the division site in response to external osmotic upshifts. Consistent with its ecological distribution, C. crescentus displays a narrow range of osmotolerance, with an upper limit of 225 mosmol/kg in minimal medium. Collectively, our findings reveal an unsuspected level of environmental regulation of cell wall protein behavior that is likely linked to an ecological adaptation.
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