ArticleEnvironmental microbiology2013
An ABC transporter and an outer membrane lipoprotein participate in posttranslational activation of type VI secretion in Pseudomonas aeruginosa.
Article in Environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 86 citations in OpenAlex.
- Functional diversity of accessory factors of the type VI secretion system.Journal of bacteriology · 2026Review
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Two cysteines control Tse1 secretion by H1-T6SS in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2025Article
- Article
- Specialized killing across the domains of life by the type VI secretion systems of Pseudomonas aeruginosa.The Biochemical journal · 2025Review
- TssL2 of T6SS2 is required for mobility, biofilm formation, wrinkly phenotype formation, and virulence of Vibrio parahaemolyticus SH112.Applied microbiology and biotechnology · 2024Article
- Initiation of H1-T6SS dueling betweenmBio · 2024Article
- Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains.Nature communications · 2024Article
- Acinetobacter type VI secretion system comprises a non-canonical membrane complex.PLoS pathogens · 2023Article
- Regulation of type VI secretion systems at the transcriptional, posttranscriptional and posttranslational level.Microbiology (Reading, England) · 2023Review
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Transcriptional organization and regulation of theMicrobiology (Reading, England) · 2023Article
- Subcellular localization of Type VI secretion system assembly in response to cell-cell contact.The EMBO journal · 2022Article
- Transcriptomic analysis ofMicrobial genomics · 2022Article
- The Type VI Secretion Systems in Plant-Beneficial Bacteria Modulate Prokaryotic and Eukaryotic Interactions in the Rhizosphere.Frontiers in microbiology · 2022Article
- Cell Envelope Stress Response in Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022Article
- Temperature-induced changes in the proteome of Pseudomonas aeruginosa during petroleum hydrocarbon degradation.Archives of microbiology · 2021Article
- Pseudomonas fluorescens F113 type VI secretion systems mediate bacterial killing and adaption to the rhizosphere microbiome.Scientific reports · 2021Article
- T6SS Mediated Stress Responses for Bacterial Environmental Survival and Host Adaptation.International journal of molecular sciences · 2021Review
- Endogenous membrane stress induces T6SS activity inProceedings of the National Academy of Sciences of the United States of America · 2021Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 8 institutions in 2 countries.
Funding
Abstract
Pseudomonas aeruginosa is capable of injecting protein toxins into other bacterial cells through one of its three type VI secretion systems (T6SSs). The activity of this T6SS is tightly regulated on the posttranslational level by phosphorylation-dependent and -independent pathways. The phosphorylation-dependent pathway consists of a Threonine kinase/phosphatase pair (PpkA/PppA) that acts on a forkhead domain-containing protein, Fha1, and a periplasmic protein, TagR, that positively regulates PpkA. In the present work, we biochemically and functionally characterize three additional proteins of the phosphorylation-dependent regulatory cascade that controls T6S activation: TagT, TagS and TagQ. We show that similar to TagR, these proteins act upstream of the PpkA/PppA checkpoint and influence phosphorylation of Fha1 and, apparatus assembly and effector export. Localization studies demonstrate that TagQ is an outer membrane lipoprotein and TagR is associated with the outer membrane. Consistent with their homology to lipoprotein outer membrane localization (Lol) components, TagT and TagS form a stable inner membrane complex with ATPase activity. However, we find that outer membrane association of T6SS lipoproteins TagQ and TssJ1, and TagR, is unaltered in a ΔtagTS background. Notably, we found that TagQ is indispensible for anchoring of TagR to the outer membrane fraction. As T6S-dependent fitness of P. aeruginosa requires TagT, S, R and Q, we conclude that these proteins likely participate in a trans-membrane signalling pathway that promotes H1-T6SS activity under optimal environmental conditions.
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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.