ArticleMolecular microbiology2015
The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- Characterization of a TatA/TatB binding site on the TatC component of theMicrobiology (Reading, England) · 2023Article
- A d-Phenylalanine-Benzoxazole Derivative Reveals the Role of the Essential Enzyme Rv3603c in the Pantothenate Biosynthetic Pathway ofACS infectious diseases · 2022Article
- The temperature-dependent expression of type II secretion system controls extracellular product secretion and virulence in mesophilicFrontiers in cellular and infection microbiology · 2022Article
- Multicopy Suppressor Analysis of Strains Lacking Cytoplasmic Peptidyl-ProlylInternational journal of molecular sciences · 2020Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
- A TonB-dependent transporter is required for secretion of protease PopC across the bacterial outer membrane.Nature communications · 2019Article
- Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.Photosynthesis research · 2018Review
- Evolution of mitochondrial TAT translocases illustrates the loss of bacterial protein transport machines in mitochondria.BMC biology · 2018Article
- Thylakoid-integrated recombinant Hcf106 participates in the chloroplast twin arginine transport system.Plant direct · 2018Article
- Precursor-Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation.Biochemistry · 2018Article
- Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.The Journal of biological chemistry · 2017Article
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- A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Comparative Analyses of Transport Proteins Encoded within the Genomes of Bdellovibrio bacteriovorus HD100 and Bdellovibrio exovorus JSS.Journal of molecular microbiology and biotechnology · 2017Article
- Assembling the Tat protein translocase.eLife · 2016Article
- TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The Tat protein export system translocates folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. The Tat system in Escherichia coli is composed of TatA, TatB and TatC proteins. TatB and TatC form an oligomeric, multivalent receptor complex that binds Tat substrates, while multiple protomers of TatA assemble at substrate-bound TatBC receptors to facilitate substrate transport. We have addressed whether oligomerisation of TatC is an absolute requirement for operation of the Tat pathway by screening for dominant negative alleles of tatC that inactivate Tat function in the presence of wild-type tatC. Single substitutions that confer dominant negative TatC activity were localised to the periplasmic cap region. The variant TatC proteins retained the ability to interact with TatB and with a Tat substrate but were unable to support the in vivo assembly of TatA complexes. Blue-native PAGE analysis showed that the variant TatC proteins produced smaller TatBC complexes than the wild-type TatC protein. The substitutions did not alter disulphide crosslinking to neighbouring TatC molecules from positions in the periplasmic cap but abolished a substrate-induced disulphide crosslink in transmembrane helix 5 of TatC. Our findings show that TatC functions as an obligate oligomer.
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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.