ArticlePLoS genetics2014
The Kil peptide of bacteriophage λ blocks Escherichia coli cytokinesis via ZipA-dependent inhibition of FtsZ assembly.
Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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61 citing papers in PubMed, 91 citations in OpenAlex.
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- Bacterial cell division protein FtsZ complexes with a phage protein to activate bacterial immunity.Nature microbiology · 2026Article
- Systematic genome-wide mapping of host determinants of bacteriophage infectivity.Cell systems · 2025Article
- KilR ofmSphere · 2025Article
- Phage provoke growth delays and SOS response induction despite CRISPR-Cas protection.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Phage-based delivery of CRISPR-associated transposases for targeted bacterial editing.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Conjugative delivery of toxin genesJournal of bacteriology · 2025Article
- In Vitro Insights into the Anti-Biofilm Potential ofAntibiotics (Basel, Switzerland) · 2025Article
- Characterization and genomic analysis of Sharanji: a jumbo bacteriophage of Escherichia coli.Virology journal · 2025Article
- A Predicted Helix-Turn-Helix Core Is Critical for Bacteriophage Kil Peptide to DisruptAntibiotics (Basel, Switzerland) · 2025Article
- Bacteriophage P1 protein Icd inhibits bacterial division by targeting FtsZ.Frontiers in microbiology · 2025Article
- Phage small proteins play large roles in phage-bacterial interactions.Current opinion in microbiology · 2024Review
- Probing Membrane-Associated Cytoskeletal Oligomers of the Bacterial Divisome by Electron Microscopy and Tomography.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Systematic and scalable genome-wide essentiality mapping to identify nonessential genes in phages.PLoS biology · 2023Article
- Identification of Toxic Proteins Encoded by Mycobacteriophage TM4 Using a Next-Generation Sequencing-Based Method.Microbiology spectrum · 2023Article
- Filamentous temperature sensitive mutant Z: a putative target to combat antibacterial resistance.RSC advances · 2023Review
- A clade of RHH proteins ubiquitous in Sulfolobales and their viruses regulates cell cycle progression.Nucleic acids research · 2023Article
- Single-Cell Approach Reveals Intercellular Heterogeneity in Phage-Producing Capacities.Microbiology spectrum · 2023Article
1 more citing papers are in PubMed but not listed here.
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9 authors at 2 institutions in 1 country.
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Abstract
Assembly of the essential, tubulin-like FtsZ protein into a ring-shaped structure at the nascent division site determines the timing and position of cytokinesis in most bacteria and serves as a scaffold for recruitment of the cell division machinery. Here we report that expression of bacteriophage λ kil, either from a resident phage or from a plasmid, induces filamentation of Escherichia coli cells by rapid inhibition of FtsZ ring formation. Mutant alleles of ftsZ resistant to the Kil protein map to the FtsZ polymer subunit interface, stabilize FtsZ ring assembly, and confer increased resistance to endogenous FtsZ inhibitors, consistent with Kil inhibiting FtsZ assembly. Cells with the normally essential cell division gene zipA deleted (in a modified background) display normal FtsZ rings after kil expression, suggesting that ZipA is required for Kil-mediated inhibition of FtsZ rings in vivo. In support of this model, point mutations in the C-terminal FtsZ-interaction domain of ZipA abrogate Kil activity without discernibly altering FtsZ-ZipA interactions. An affinity-tagged-Kil derivative interacts with both FtsZ and ZipA, and inhibits sedimentation of FtsZ filament bundles in vitro. Together, these data inspire a model in which Kil interacts with FtsZ and ZipA in the cell to prevent FtsZ assembly into a coherent, division-competent ring structure. Phage growth assays show that kil+ phage lyse ∼30% later than kil mutant phage, suggesting that Kil delays lysis, perhaps via its interaction with FtsZ and ZipA.
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