ArticleThe Journal of cell biology2012
Stoichiometry for binding and transport by the twin arginine translocation system.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- 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
- Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.Communications biology · 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
- Liquid-Liquid Phase Separation Phenomenon on Protein Sorting Within Chloroplasts.Frontiers in physiology · 2021Review
- 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
- Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.Photosynthesis research · 2018Review
- Thylakoid-integrated recombinant Hcf106 participates in the chloroplast twin arginine transport system.Plant direct · 2018Article
- The Tat protein transport system: intriguing questions and conundrums.FEMS microbiology letters · 2018Review
- Precursor-Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation.Biochemistry · 2018Article
- Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.Scientific reports · 2018Article
- A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.Biophysical journal · 2017Article
- The peroxisomal matrix protein translocon is a large cavity-forming protein assembly into which PEX5 protein enters to release its cargo.The Journal of biological chemistry · 2017Article
- How to achieve Tat transport with alien TatA.Scientific reports · 2017Article
- Identification of Putative Substrates of SEC2, a Chloroplast Inner Envelope Translocase.Plant physiology · 2017Article
- 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
2 authors at 1 institution in 1 country.
Funding
Abstract
Twin arginine translocation (Tat) systems transport large folded proteins across sealed membranes. Tat systems accomplish this feat with three membrane components organized in two complexes. In thylakoid membranes, cpTatC and Hcf106 comprise a large receptor complex containing an estimated eight cpTatC-Hcf106 pairs. Protein transport occurs when Tha4 joins the receptor complex as an oligomer of uncertain size that is thought to form the protein-conducting structure. Here, binding analyses with intact membranes or purified complexes indicate that each receptor complex could bind eight precursor proteins. Kinetic analysis of translocation showed that each precursor-bound site was independently functional for transport, and, with sufficient Tha4, all sites were concurrently active for transport. Tha4 titration determined that ∼26 Tha4 protomers were required for transport of each OE17 (oxygen-evolving complex subunit of 17 kD) precursor protein. Our results suggest that, when fully saturated with precursor proteins and Tha4, the Tat translocase is an ∼2.2-megadalton complex that can individually transport eight precursor proteins or cooperatively transport multimeric precursors.
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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.