ArticleThe Biochemical journal2014
Biochemical analysis of TssK, a core component of the bacterial Type VI secretion system, reveals distinct oligomeric states of TssK and identifies a TssK-TssFG subcomplex.
Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 52 citations in OpenAlex.
- No fitness cost entailed by type VI secretion system synthesis, assembly, contraction, or disassembly in enteroaggregativeJournal of bacteriology · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- The accessory protein TagV is required for full Type VI secretion system activity in Serratia marcescens.Molecular microbiology · 2023Article
- The Antivirulence Activity of Umbelliferone and Its Protective Effect againstInternational journal of molecular sciences · 2022Article
- Article
- Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.PloS one · 2021Article
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- Article
- Fur-Dam Regulatory Interplay at an Internal Promoter of the Enteroaggregative Escherichia coli Type VI SecretionJournal of bacteriology · 2020Article
- Structure and Activity of the Type VI Secretion System.Microbiology spectrum · 2019Review
- Role and Recruitment of the TagL Peptidoglycan-Binding Protein during Type VI Secretion System Biogenesis.Journal of bacteriology · 2019Article
- Type VI Secretion System in PathogenicFrontiers in microbiology · 2019Review
- Two Functionally Deviating Type 6 Secretion Systems Occur in the Nitrogen-Fixing EndophyteFrontiers in microbiology · 2019Article
- Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy.Nature communications · 2018Article
- Biogenesis and structure of a type VI secretion baseplate.Nature microbiology · 2018Article
- Structural insights into the function of type VI secretion system TssA subunits.Nature communications · 2018Article
- In vivo TssA proximity labelling during type VI secretion biogenesis reveals TagA as a protein that stops and holds the sheath.Nature microbiology · 2018Article
- Bacterial symbionts use a type VI secretion system to eliminate competitors in their natural host.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- TssA from Burkholderia cenocepacia: expression, purification, crystallization and crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Cryo-EM reconstruction of Type VI secretion system baseplate and sheath distal end.The EMBO journal · 2018Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Gram-negative bacteria use the Type VI secretion system (T6SS) to inject toxic proteins into rival bacteria or eukaryotic cells. However, the mechanism of the T6SS is incompletely understood. In the present study, we investigated a conserved component of the T6SS, TssK, using the antibacterial T6SS of Serratia marcescens as a model system. TssK was confirmed to be essential for effector secretion by the T6SS. The native protein, although not an integral membrane protein, appeared to localize to the inner membrane, consistent with its presence within a membrane-anchored assembly. Recombinant TssK purified from S. marcescens was found to exist in several stable oligomeric forms, namely trimer, hexamer and higher-order species. Native-level purification of TssK identified TssF and TssG as interacting proteins. TssF and TssG, conserved T6SS components of unknown function, were required for T6SS activity, but not for correct localization of TssK. A complex containing TssK, TssF and TssG was subsequently purified in vitro, confirming that these three proteins form a new subcomplex within the T6SS. Our findings provide new insight into the T6SS assembly, allowing us to propose a model whereby TssK recruits TssFG into the membrane-associated T6SS complex and different oligomeric states of TssK may contribute to the dynamic mechanism of the system.
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