ArticlePloS one2013
Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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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.
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Who cites it
38 citing papers in PubMed, 61 citations in OpenAlex.
- Review
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.Scientific reports · 2024Article
- Aberrant Topologies of Bacterial Membrane Proteins Revealed by High Sensitivity Fluorescence Labelling.Journal of molecular biology · 2024Article
- Defining Assembly Pathways by Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Characterization of a TatA/TatB binding site on the TatC component of theMicrobiology (Reading, England) · 2023Article
- New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon.Molecular microbiology · 2022Article
- Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria.Microbial cell (Graz, Austria) · 2022Review
- Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.Communications biology · 2022Article
- Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.Scientific reports · 2022Article
- Electrochromic shift supports the membrane destabilization model of Tat-mediated transport and shows ion leakage during Sec transport.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Dynamics of Bacterial Signal Recognition Particle at a Single Molecule Level.Frontiers in microbiology · 2021Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Clustering as a Means To Control Nitrate Respiration Efficiency and Toxicity in Escherichia coli.mBio · 2019Article
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- A Potential Late Stage Intermediate of Twin-Arginine Dependent Protein Translocation inFrontiers in microbiology · 2019Article
- Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.Photosynthesis research · 2018Review
- The Tat protein transport system: intriguing questions and conundrums.FEMS microbiology letters · 2018Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The twin-arginine translocation (Tat) pathway guides fully folded proteins across membranes of bacteria, archaea and plant chloroplasts. In Escherichia coli, Tat-specific transport is executed in a still largely unknown manner by three functionally diverse membrane proteins, termed TatA, TatB, and TatC. In order to follow the intracellular distribution of the TatABC proteins in live E. coli cells, we have individually expressed fluorophore-tagged versions of each Tat protein in addition to a set of chromosomally encoded TatABC proteins. In this way, a Tat translocase could form from the native TatABC proteins and be visualized via the association of a fluorescent Tat variant. A functionally active TatA-green fluorescent protein fusion was found to re-locate from a uniform distribution in the membrane into a few clusters preferentially located at the cell poles. Clustering was absolutely dependent on the co-expression of functional Tat substrates, the proton-motive force, and the cognate TatBC subunits. Likewise, polar cluster formation of a functional TatB-mCherry fusion required TatA and TatC and that of a functional TatC-mCherry fusion a functional Tat substrate. Furthermore we directly demonstrate the co-localization of TatA and TatB in the same fluorescent clusters. Our collective results are consistent with distinct Tat translocation sites dynamically forming in vivo in response to newly synthesized Tat substrates.
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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.