ReviewThe protein journal2019
Transport of Folded Proteins by the Tat System.
Review in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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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
46 citing papers in PubMed, 90 citations in OpenAlex.
- Are Signal Peptides Hidden Regulators of Neurodegenerative Disease?Biomedicines · 2026Review
- Pst and Tat Systems Are Essential forMicroorganisms · 2026Article
- The peroxisomal importomer can accommodate an intrinsically disordered protein of 1247 residues.Histochemistry and cell biology · 2026Article
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- The complexities of respiratory chain biogenesis and maintenance in yeast mitochondria.Protein science : a publication of the Protein Society · 2026Review
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- Repurposing the bacterial surface display technology for drug delivery.Advanced drug delivery reviews · 2025Review
- Outer Membrane Vesicles as a Versatile Platform for Vaccine Development: Engineering Strategies, Applications and Challenges.Journal of extracellular vesicles · 2025Review
- Protein Translocation Control inBiomolecules · 2025Article
- Signal Peptides: From Molecular Mechanisms to Applications in Protein and Vaccine Engineering.Biomolecules · 2025Review
- Synergistic Engineering of the Twin-Arginine Translocation (Tat) Pathway and Membrane Capacity Enhances Extracellular Production of Amylosucrase inMicroorganisms · 2025Article
- HNP-1: From Structure to Application Thanks to Multifaceted Functions.Microorganisms · 2025Review
- Article
- The Freshwater CyanobacteriumPlants (Basel, Switzerland) · 2024Article
- The Construction of an Environmentally Friendly Super-Secreting Strain ofInternational journal of molecular sciences · 2024Article
- N-Terminal Sequences of Signal Peptides Assuming Critical Roles in Expression of Heterologous Proteins inMicroorganisms · 2024Article
- A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.Scientific reports · 2024Article
- Bacillus subtilis: current and future modification strategies as a protein secreting factory.World journal of microbiology & biotechnology · 2024Review
- Towards solving the mystery of peroxisomal matrix protein import.Trends in cell biology · 2024Review
- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The twin-arginine protein translocation (Tat) system has been characterized in bacteria, archaea and the chloroplast thylakoidal membrane. This system is distinct from other protein transport systems with respect to two key features. Firstly, it accepts cargo proteins with an N-terminal signal peptide that carries the canonical twin-arginine motif, which is essential for transport. Second, the Tat system only accepts and translocates fully folded cargo proteins across the respective membrane. Here, we review the core essential features of folded protein transport via the bacterial Tat system, using the three-component TatABC system of Escherichia coli and the two-component TatAC systems of Bacillus subtilis as the main examples. In particular, we address features of twin-arginine signal peptides, the essential Tat components and how they assemble into different complexes, mechanistic features and energetics of Tat-dependent protein translocation, cytoplasmic chaperoning of Tat cargo proteins, and the remarkable proofreading capabilities of the Tat system. In doing so, we present the current state of our understanding of Tat-dependent protein translocation across biological membranes, which may serve as a lead for future investigations.
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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.