ArticleThe Journal of biological chemistry2014
Coevolution of the ATPase ClpV, the sheath proteins TssB and TssC, and the accessory protein TagJ/HsiE1 distinguishes type VI secretion classes.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- From gut colonization to recurrence:Gut microbes · 2026Review
- Review
- Functional diversity of accessory factors of the type VI secretion system.Journal of bacteriology · 2026Review
- TheMicroorganisms · 2026Article
- The Competitive Edge: T6SS-Mediated Interference Competition byMicroorganisms · 2025Review
- Integrative omics analysis reveals distinct adaptations of bongkrekic acid producingFrontiers in microbiology · 2025Article
- Molecular dynamic simulations to assess the structural variability of ClpV fromFrontiers in bioinformatics · 2025Article
- Structural and Functional Characterization of a Putative Type VI Secretion System Protein inEvolutionary bioinformatics online · 2025Article
- Symbiotic T6SS affects horizontal transmission ofISME communications · 2025Article
- The Role of ClpV in the Physiology and Pathogenicity ofMicroorganisms · 2024Article
- No fitness cost entailed by type VI secretion system synthesis, assembly, contraction, or disassembly in enteroaggregativeJournal of bacteriology · 2023Article
- Acinetobacter type VI secretion system comprises a non-canonical membrane complex.PLoS pathogens · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Bacterial type VI secretion system (T6SS): an evolved molecular weapon with diverse functionality.Biotechnology letters · 2023Review
- Uncovering the Secretion Systems ofAntibiotics (Basel, Switzerland) · 2023Review
- The Missing Pieces: The Role of Secretion Systems inBiomolecules · 2023Review
- Subcellular localization of Type VI secretion system assembly in response to cell-cell contact.The EMBO journal · 2022Article
- The ecological impact of a bacterial weapon: microbial interactions and the Type VI secretion system.FEMS microbiology reviews · 2021Article
- Putative RNA Ligase RtcB Affects the Switch between T6SS and T3SS inInternational journal of molecular sciences · 2021Article
- Evolution of Interbacterial Antagonism in Bee Gut Microbiota Reflects Host and Symbiont Diversification.mSystems · 2021Article
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6 authors.
Funding
Abstract
The type VI secretion system (T6SS) is a bacterial nanomachine for the transport of effector molecules into prokaryotic and eukaryotic cells. It involves the assembly of a tubular structure composed of TssB and TssC that is similar to the tail sheath of bacteriophages. The sheath contracts to provide the energy needed for effector delivery. The AAA(+) ATPase ClpV disassembles the contracted sheath, which resets the systems for reassembly of an extended sheath that is ready to fire again. This mechanism is crucial for T6SS function. In Vibrio cholerae, ClpV binds the N terminus of TssC within a hydrophobic groove. In this study, we resolved the crystal structure of the N-terminal domain of Pseudomonas aeruginosa ClpV1 and observed structural alterations in the hydrophobic groove. The modification in the ClpV1 groove is matched by a change in the N terminus of TssC, suggesting the existence of distinct T6SS classes. An accessory T6SS component, TagJ/HsiE, exists predominantly in one of the classes. Using bacterial two-hybrid approaches, we showed that the P. aeruginosa homolog HsiE1 interacts strongly with ClpV1. We then resolved the crystal structure of HsiE1 in complex with the N terminus of HsiB1, a TssB homolog and component of the contractile sheath. Phylogenetic analysis confirmed that these differences distinguish T6SS classes that resulted from a functional co-evolution between TssB, TssC, TagJ/HsiE, and ClpV. The interaction of TagJ/HsiE with the sheath as well as with ClpV suggests an alternative mode of disassembly in which HsiE recruits the ATPase to the sheath.
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