ArticleThe EMBO journal2019
Diverse roles of TssA-like proteins in the assembly of bacterial type VI secretion systems.
Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed.
- Functional diversity of accessory factors of the type VI secretion system.Journal of bacteriology · 2026Review
- Review
- Gene-in-gene coding generates dual-isoform Fha condensates to control type VI secretion system assembly.Nature communications · 2026Article
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Biophysical characterization of Eag chaperones suggests the mechanism of effector transmembrane domain release.Nature communications · 2026Article
- TssW-PpkA-Fha axis controls the positioning and initiation of the type VI secretion system inmBio · 2025Article
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- Initiation of H1-T6SS dueling betweenmBio · 2024Article
- Bactericidal effectors of themBio · 2024Article
- T6SS nuclease effectors inJournal of bacteriology · 2024Article
- Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains.Nature communications · 2024Article
- Regulation of type VI secretion systems at the transcriptional, posttranscriptional and posttranslational level.Microbiology (Reading, England) · 2023Review
- Qualitative and Quantitative Methods to Measure Antibacterial Activity Resulting from Bacterial Competition.Bio-protocol · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- The T6SS-Dependent Effector Re78 ofBiology · 2023Article
- Effectiveness of Pseudomonas aeruginosa type VI secretion system relies on toxin potency and type IV pili-dependent interaction.PLoS pathogens · 2023Article
- Bacterial type VI secretion system (T6SS): an evolved molecular weapon with diverse functionality.Biotechnology letters · 2023Review
- The type-VI secretion system of the beneficial symbiontMicrobiology (Reading, England) · 2023Review
- PandemicLife science alliance · 2023Article
- Type VI Secretion Systems: Environmental and Intra-host Competition of Vibrio cholerae.Advances in experimental medicine and biology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Protein translocation by the bacterial type VI secretion system (T6SS) is driven by a rapid contraction of a sheath assembled around a tube with associated effectors. Here, we show that TssA-like or TagA-like proteins with a conserved N-terminal domain and varying C-terminal domains can be grouped into at least three distinct classes based on their role in sheath assembly. The proteins of the first class increase speed and frequency of sheath assembly and form a stable dodecamer at the distal end of a polymerizing sheath. The proteins of the second class localize to the cell membrane and block sheath polymerization upon extension across the cell. This prevents excessive sheath polymerization and bending, which may result in sheath destabilization and detachment from its membrane anchor and thus result in failed secretion. The third class of these proteins localizes to the baseplate and is required for initiation of sheath assembly. Our work shows that while various proteins share a conserved N-terminal domain, their roles in T6SS biogenesis are fundamentally different.
Indexed as
Identifiers
What OpenQuestion holds
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.