ArticleThe Journal of biological chemistry2011
Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.
Article in The Journal of biological chemistry, 2011. 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, 48 citations in OpenAlex.
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Cross-Species Functional Conservation and Possible Origin of the N-Terminal Specificity Domain of Mitochondrial Presequences.Frontiers in plant science · 2020Article
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Protein Expression Modifications in Phage-Resistant Mutants of Aeromonas salmonicida after AS-A Phage Treatment.Antibiotics (Basel, Switzerland) · 2018Article
- Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.Scientific reports · 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
- A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.Biophysical journal · 2017Article
- In vivo experiments do not support the charge zipper model for Tat translocase assembly.eLife · 2017Article
- The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.The Journal of biological chemistry · 2017Article
- TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases.The Journal of biological chemistry · 2015Article
- Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).The Journal of biological chemistry · 2015Review
- Initial assembly steps of a translocase for folded proteins.Nature communications · 2015Article
- Illumination of growth, division and secretion by metabolic labeling of the bacterial cell surface.FEMS microbiology reviews · 2015Review
- TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.PloS one · 2015Article
- Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly.The Journal of cell biology · 2014Article
- Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure.PloS one · 2014Article
- Structural model for the protein-translocating element of the twin-arginine transport system.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Mapping the signal peptide binding and oligomer contact sites of the core subunit of the pea twin arginine protein translocase.The Plant cell · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Twin-arginine translocation (Tat) is a unique protein transport pathway in bacteria, archaea, and plastids. It mediates the transmembrane transport of fully folded proteins, which harbor a consensus twin-arginine motif in their signal sequences. In Gram-negative bacteria and plant chloroplasts, three membrane proteins, named TatA, TatB, and TatC, are required to enable Tat translocation. Available data suggest that TatA assembles into oligomeric pore-like structures that might function as the protein conduit across the lipid bilayer. Using site-specific photo-cross-linking, we have investigated the molecular environment of TatA under resting and translocating conditions. We find that monomeric TatA is an early interacting partner of functionally targeted Tat substrates. This interaction with TatA likely precedes translocation of Tat substrates and is influenced by the proton-motive force. It strictly depends on the presence of TatB and TatC, the latter of which is shown to make contacts with the transmembrane helix of TatA.
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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.