ArticleProceedings of the National Academy of Sciences of the United States of America2015
FtsZ filament capping by MciZ, a developmental regulator of bacterial division.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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.
- Bacterial cell division protein FtsZ complexes with a phage protein to activate bacterial immunity.Nature microbiology · 2026Article
- FtsZ as a novel target for antibiotics development: Promises and challenges.Acta pharmaceutica Sinica. B · 2025Review
- Transient inhibition of cell division in competent pneumococcal cells results from deceleration of the septal peptidoglycan complex.Nature communications · 2025Article
- Article
- Large Roles of Small Proteins.Annual review of microbiology · 2024Review
- Manipulating Microbial Cell Morphology for the Sustainable Production of Biopolymers.Polymers · 2024Review
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023Article
- Filamentous temperature sensitive mutant Z: a putative target to combat antibacterial resistance.RSC advances · 2023Review
- FtsZ phosphorylation brings about growth arrest upon DNA damage inFASEB bioAdvances · 2023Article
- MipZ caps the plus-end of FtsZ polymers to promote their rapid disassembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Filamentous morphology of bacterial pathogens: regulatory factors and control strategies.Applied microbiology and biotechnology · 2022Review
- The Search for Antibacterial Inhibitors Targeting Cell Division Protein FtsZ at Its Nucleotide and Allosteric Binding Sites.Biomedicines · 2022Review
- Mapping functional regions of essential bacterial proteins with dominant-negative protein fragments.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics.PLoS biology · 2022Article
- Designing efficient genetic code expansion in Bacillus subtilis to gain biological insights.Nature communications · 2021Article
- Article
- Single-molecule imaging reveals that Z-ring condensation is essential for cell division in Bacillus subtilis.Nature microbiology · 2021Article
- Targeting the Achilles Heel of FtsZ: The Interdomain Cleft.Frontiers in microbiology · 2021Review
- SR7 - a dual-function antisense RNA fromRNA biology · 2021Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Cytoskeletal structures are dynamically remodeled with the aid of regulatory proteins. FtsZ (filamentation temperature-sensitive Z) is the bacterial homolog of tubulin that polymerizes into rings localized to cell-division sites, and the constriction of these rings drives cytokinesis. Here we investigate the mechanism by which the Bacillus subtilis cell-division inhibitor, MciZ (mother cell inhibitor of FtsZ), blocks assembly of FtsZ. The X-ray crystal structure reveals that MciZ binds to the C-terminal polymerization interface of FtsZ, the equivalent of the minus end of tubulin. Using in vivo and in vitro assays and microscopy, we show that MciZ, at substoichiometric levels to FtsZ, causes shortening of protofilaments and blocks the assembly of higher-order FtsZ structures. The findings demonstrate an unanticipated capping-based regulatory mechanism for FtsZ.
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Registered trials
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.