ArticleThe Journal of biological chemistry2013
The HsiB1C1 (TssB-TssC) complex of the Pseudomonas aeruginosa type VI secretion system forms a bacteriophage tail sheathlike structure.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 82 citations in OpenAlex.
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- Integrative Systems-Level Transcriptomic Network Analysis Identifies Candidate Genes Associated with Biofilm Formation and Virulence inInternational journal of molecular sciences · 2026Article
- The Pseudomonas aeruginosa Tse4 toxin assembles ion-selective and voltage-sensitive ion channels to couple membrane depolarisation with K+ efflux.PLoS pathogens · 2025Article
- Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains.Nature communications · 2024Article
- Article
- Protein-Protein Interactions: Yeast Two Hybrid.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Bacterial type VI secretion system (T6SS): an evolved molecular weapon with diverse functionality.Biotechnology letters · 2023Review
- RpoN/Sfa2-dependent activation of the Pseudomonas aeruginosa H2-T6SS and its cognate arsenal of antibacterial toxins.Nucleic acids research · 2022Article
- Recruitment of Mobile Genetic Elements for Diverse Cellular Functions in Prokaryotes.Frontiers in molecular biosciences · 2022Review
- Structure of a bacterial Rhs effector exported by the type VI secretion system.PLoS pathogens · 2022Article
- The ecological impact of a bacterial weapon: microbial interactions and the Type VI secretion system.FEMS microbiology reviews · 2021Article
- Endogenous membrane stress induces T6SS activity inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Impacts of Ser/Thr Protein Kinase Stk1 on the Proteome, Twitching Motility, and Competitive Advantage inFrontiers in microbiology · 2021Article
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- Effector loading onto the VgrG carrier activates type VI secretion system assembly.EMBO reports · 2020Article
- HSI-II Gene Cluster ofFrontiers in microbiology · 2020Article
- Article
- Role of Recipient Susceptibility Factors During Contact-Dependent Interbacterial Competition.Frontiers in microbiology · 2020Review
- Crosstalk Between Type VI Secretion System and Mobile Genetic Elements.Frontiers in molecular biosciences · 2019Review
- Type VI Secretion System in PathogenicFrontiers in microbiology · 2019Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Protein secretion systems in Gram-negative bacteria evolved into a variety of molecular nanomachines. They are related to cell envelope complexes, which are involved in assembly of surface appendages or transport of solutes. They are classified as types, the most recent addition being the type VI secretion system (T6SS). The T6SS displays similarities to bacteriophage tail, which drives DNA injection into bacteria. The Hcp protein is related to the T4 bacteriophage tail tube protein gp19, whereas VgrG proteins structurally resemble the gp27/gp5 puncturing device of the phage. The tube and spike of the phage are pushed through the bacterial envelope upon contraction of a tail sheath composed of gp18. In Vibrio cholerae it was proposed that VipA and VipB assemble into a tail sheathlike structure. Here we confirm these previous data by showing that HsiB1 and HsiC1 of the Pseudomonas aeruginosa H1-T6SS assemble into tubules resulting from stacking of cogwheel-like structures showing predominantly 12-fold symmetry. The internal diameter of the cogwheels is ~100 Å, which is large enough to accommodate an Hcp tube whose external diameter has been reported to be 85 Å. The N-terminal 212 residues of HsiC1 are sufficient to form a stable complex with HsiB1, but the C terminus of HsiC1 is essential for the formation of the tubelike structure. Bioinformatics analysis suggests that HsiC1 displays similarities to gp18-like proteins in its C-terminal region. In conclusion, we provide further structural and mechanistic insights into the T6SS and show that a phage sheathlike structure is likely to be a conserved element across all T6SSs.
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