ArticleProceedings of the National Academy of Sciences of the United States of America2009
RodZ, a component of the bacterial core morphogenic apparatus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
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Who cites it
107 citing papers in PubMed, 172 citations in OpenAlex.
- RodZ acts through MreBCD to activate the elongasome inJournal of bacteriology · 2026Article
- A broadly conserved gram-positive lipoprotein regulates cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Twin-arginine transport complex plays an essential role inMolecular biology of the cell · 2026Article
- Maintenance of cytoplasmic and membrane densities shapes cellular geometry in Escherichia coli.Nature communications · 2025Article
- Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025Article
- OpgH is an essential regulator ofmBio · 2024Article
- An outer membrane porin-lipoprotein complex modulates elongasome movement to establish cell curvature in Rhodospirillum rubrum.Nature communications · 2024Article
- Fluorescent riboswitch-controlled biosensors for the genome scale analysis of metabolic pathways.Scientific reports · 2024Article
- The role of GpsB inmBio · 2024Article
- A dynamic bactofilin cytoskeleton cooperates with an M23 endopeptidase to control bacterial morphogenesis.eLife · 2024Article
- Relationship between the Rod complex and peptidoglycan structure in Escherichia coli.MicrobiologyOpen · 2023Article
- A role for the Gram-negative outer membrane in bacterial shape determination.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- A conserved zinc-binding site inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- A role for the Gram-negative outer membrane in bacterial shape determination.bioRxiv : the preprint server for biology · 2023Article
- Plasticity in the cell division processes of obligate intracellular bacteria.Frontiers in cellular and infection microbiology · 2023Review
- Enzyme 1 of the phosphoenolpyruvate:sugar phosphotransferase system is involved in resistance to MreB disruption in wild-type and ∆envC cells.Molecular microbiology · 2022Article
- Roles of RodZ and class A PBP1b in the assembly and regulation of the peripheral peptidoglycan elongasome in ovoid-shaped cells of Streptococcus pneumoniae D39.Molecular microbiology · 2022Article
- What Is Motion? Recent Advances in the Study of Molecular Movement Patterns of the Peptidoglycan Synthesis Machines.Journal of bacteriology · 2022Review
- Cell density-dependent antibiotic tolerance to inhibition of the elongation machinery requires fully functional PBP1B.Communications biology · 2022Article
47 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 4 countries.
Funding
Abstract
The molecular basis of bacterial cell morphogenesis remains largely an open question. Here we discover a morphogenic protein, RodZ, which is widely conserved across the bacterial kingdom. In Caulobacter crescentus, RodZ is essential for viability and is involved in all aspects of this organism's complex morphology. Depletion or over-production of RodZ results in grossly misshapen cells with stalk defects. RodZ exhibits a localization pattern during the cell cycle corresponding to sites of active peptidoglycan synthesis. The temporal transition of RodZ between patchy/helical and mid-cell localization mimics and depends on the actin-like MreB cytoskeleton. In Escherichia coli, an organism with a distinct mode of growth and MreB localization dynamics, RodZ follows MreB and retains its crucial role in cell morphogenesis, demonstrating conservation of function. Genomic analysis shows that RodZ represents an ancient function unique to bacteria. Multiple sequence alignment of 143 RodZ sequences from species across bacterial phyla identifies an N-terminal cytoplasmic domain with a helix-turn-helix motif, a transmembrane sequence, and a previously unidentified, conserved periplasmic or extracellular C-terminal domain. Both the N- and C-terminal domains are important for function, with the N-terminal domain containing localization determinants. This study uncovers a key missing player in the cytoskeleton-based growth machinery enabling heritable and defined cellular forms in bacteria.
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