ArticleProceedings of the National Academy of Sciences of the United States of America2013
Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 79 citations in OpenAlex.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- Review
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- Role of the Multicopper Oxidase CueO in Copper Homeostasis Under Anaerobic Conditions in Enterobacteria.Molecular microbiology · 2025Article
- 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
- How Do Biomolecules Cross the Cell Membrane?Accounts of chemical research · 2022Article
- Dynamics of Proteins and Macromolecular Machines in Escherichia coli.EcoSal Plus · 2021Review
- Article
- 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
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The twin-arginine translocation (Tat) machinery transports folded proteins across the cytoplasmic membrane of bacteria and the thylakoid membrane of chloroplasts. It has been inferred that the Tat translocation site is assembled on demand by substrate-induced association of the protein TatA. We tested this model by imaging YFP-tagged TatA expressed at native levels in living Escherichia coli cells in the presence of low levels of the TatA paralogue TatE. Under these conditions the TatA-YFP fusion supports full physiological Tat transport activity. In agreement with the TatA association model, raising the number of transport-competent substrate proteins within the cell leads to an increase in the number of large TatA complexes present. Formation of these complexes requires both a functional TatBC substrate receptor and the transmembrane proton motive force (PMF). Removing the PMF causes TatA complexes to dissociate, except in strains with impaired Tat transport activity. Based on these observations we propose that TatA assembly reaches a critical point at which oligomerization can be reversed only by substrate transport. In contrast to TatA-YFP, the oligomeric states of TatB-YFP and TatC-YFP fusions are not affected by substrate or the PMF, although TatB-YFP oligomerization does require TatC.
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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.