ArticleThe EMBO journal2004
Coordinating assembly and export of complex bacterial proteins.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed.
- Genetic dissection of formate hydrogenlyase-2 function: a metalloenzyme involved in bacterial hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- A widely-occurring family of pore-forming effectors broadens the impact of the Serratia Type VI secretion system.The EMBO journal · 2025Article
- Cleavage cascade of the sigma regulator FecR orchestrates TonB-dependent signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase.Microbiology (Reading, England) · 2024Article
- Protein-Protein Interaction: Bacterial Two Hybrid.Methods in molecular biology (Clifton, N.J.) · 2024Article
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Highly efficient export of a disulfide-bonded protein to the periplasm and medium by the Tat pathway using CyDisCo in Escherichia coli.MicrobiologyOpen · 2023Article
- Analysis of the Brucella suis Twin Arginine Translocation System and Its Substrates Shows That It Is Essential for Viability.Infection and immunity · 2023Article
- Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.Scientific reports · 2022Article
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism.Journal of bacteriology · 2020Article
- The plant pathogen Pectobacterium atrosepticum contains a functional formate hydrogenlyase-2 complex.Molecular microbiology · 2019Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- DMSO Reductase Family: Phylogenetics and Applications of Extremophiles.International journal of molecular sciences · 2019Review
- A bacterial signaling system regulates noise to enable bet hedging.Current genetics · 2019Review
- The Di-iron RIC Protein (YtfE) of Escherichia coli Interacts with the DNA-Binding Protein from Starved Cells (Dps) To Diminish RIC Protein-Mediated Redox Stress.Journal of bacteriology · 2018Article
- Secretion of recombinant proteins fromEngineering in life sciences · 2018Review
- Probing the quality control mechanism of theThe Journal of biological chemistry · 2018Article
- A Bacterial Adenylate Cyclase-Based Two-Hybrid System Compatible with GatewayMethods in molecular biology (Clifton, N.J.) · 2018Article
- Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli twin-arginine protein transport (Tat) system is a molecular machine dedicated to the translocation of fully folded substrate proteins across the energy-transducing inner membrane. Complex cofactor-containing Tat substrates, such as the model (NiFe) hydrogenase-2 and trimethylamine N-oxide reductase (TorA) systems, acquire their redox cofactors prior to export from the cell and require to be correctly assembled before transport can proceed. It is likely, therefore, that cellular mechanisms exist to prevent premature export of immature substrates. Using a combination of genetic and biochemical approaches including gene knockouts, signal peptide swapping, complementation, and site-directed mutagenesis, we highlight here this crucial 'proofreading' or 'quality control' activity in operation during assembly of complex endogenous Tat substrates. Our experiments successfully uncouple the Tat transport and cofactor-insertion activities of the TorA-specific chaperone TorD and demonstrate unequivocally that TorD recognises the TorA twin-arginine signal peptide. It is proposed that some Tat signal peptides operate in tandem with cognate binding chaperones to orchestrate the assembly and transport of complex enzymes.
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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.