ArticleThe Journal of biological chemistry2015
Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Bacterial cell division protein FtsZ complexes with a phage protein to activate bacterial immunity.Nature microbiology · 2026Article
- KilR ofmSphere · 2025Article
- Conjugative delivery of toxin genesJournal of bacteriology · 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
- Article
- Filamentous temperature sensitive mutant Z: a putative target to combat antibacterial resistance.RSC advances · 2023Review
- Bacterial division ring stabilizing ZapA versus destabilizing SlmA modulate FtsZ switching between biomolecular condensates and polymers.Open biology · 2023Article
- A mechanism of salt bridge-mediated resistance to FtsZ inhibitor PC190723 revealed by a cell-based screen.Molecular biology of the cell · 2023Article
- A clade of RHH proteins ubiquitous in Sulfolobales and their viruses regulates cell cycle progression.Nucleic acids research · 2023Article
- Investigating the effect of bacteriophages on bacterial FtsZ localisation.Frontiers in cellular and infection microbiology · 2022Article
- A newly identified prophage-encoded gene,Journal of bacteriology · 2021Article
- FtsZ Interactions and Biomolecular Condensates as Potential Targets for New Antibiotics.Antibiotics (Basel, Switzerland) · 2021Review
- Targeting the Achilles Heel of FtsZ: The Interdomain Cleft.Frontiers in microbiology · 2021Review
- Bacteriophage SP01 Gene Product 56 Inhibits Bacillus subtilis Cell Division by Interacting with FtsL and Disrupting Pbp2B and FtsW Recruitment.Journal of bacteriology · 2020Article
- Purification and characterization of FtsZ from the citrus canker pathogen Xanthomonas citri subsp. citri.MicrobiologyOpen · 2019Article
- Bacterial FtsZ protein forms phase-separated condensates with its nucleoid-associated inhibitor SlmA.EMBO reports · 2019Article
- Cross-Regulation between Bacteria and Phages at a Posttranscriptional Level.Microbiology spectrum · 2018Review
- OxyS small RNA induces cell cycle arrest to allow DNA damage repair.The EMBO journal · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The effects of Kil peptide from bacteriophage λ on the assembly of Escherichia coli FtsZ into one subunit thick protofilaments were studied using combined biophysical and biochemical methods. Kil peptide has recently been identified as the factor from bacteriophage λ responsible for the inhibition of bacterial cell division during lytic cycle, targeting FtsZ polymerization. Here, we show that this antagonist blocks FtsZ assembly into GTP-dependent protofilaments, producing a wide distribution of smaller oligomers compared with the average size of the intact protofilaments. The shortening of FtsZ protofilaments by Kil is detectable at concentrations of the peptide in the low micromolar range, the mid-point of the inhibition being close to its apparent affinity for GDP-bound FtsZ. This antagonist not only interferes with FtsZ assembly but also reverses the polymerization reaction. The negative regulation by Kil significantly reduces the GTPase activity of FtsZ protofilaments, and FtsZ polymers assembled in guanosine-5'-[(α,β)-methyleno]triphosphate are considerably less sensitive to Kil. Our results suggest that, at high concentrations, Kil may use an inhibition mechanism involving the sequestration of FtsZ subunits, similar to that described for other inhibitors like the SOS response protein SulA or the moonlighting enzyme OpgH. This mechanism is different from those employed by the division site selection antagonists MinC and SlmA. This work provides new insight into the inhibition of FtsZ assembly by phages, considered potential tools against bacterial infection.
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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.