The Bacterial Twin-arginine Translocation Pathway

Overview

Journal Annu Rev Microbiol

Publisher Annual Reviews

Specialty Microbiology

Date 2006 Jun 8

PMID 16756481

Citations 134

Authors

Philip A Lee

Danielle Tullman-Ercek

George Georgiou

Affiliations

Soon will be listed here.

Abstract

The twin-arginine translocation (Tat) pathway is responsible for the export of folded proteins across the cytoplasmic membrane of bacteria. Substrates for the Tat pathway include redox enzymes requiring cofactor insertion in the cytoplasm, multimeric proteins that have to assemble into a complex prior to export, certain membrane proteins, and proteins whose folding is incompatible with Sec export. These proteins are involved in a diverse range of cellular activities including anaerobic metabolism, cell envelope biogenesis, metal acquisition and detoxification, and virulence. The Escherichia coli translocase consists of the TatA, TatB, and TatC proteins, but little is known about the precise sequence of events that leads to protein translocation, the energetic requirements, or the mechanism that prevents the export of misfolded proteins. Owing to the unique characteristics of the pathway, it holds promise for biotechnological applications.

Citing Articles

Disruption and adaptation: infant gut microbiota's dynamic response to SARS-CoV-2 infection.

Zhu L, Zhao L, Zhu Y, Xu X, Lin J, Duan Y Microbiome. 2025; 13(1):72.

PMID: 40069800 PMC: 11895207. DOI: 10.1186/s40168-025-02029-6.

Advancements in Escherichia coli secretion systems for enhanced recombinant protein production.

Lokireddy S, Kunchala S, Vadde R World J Microbiol Biotechnol. 2025; 41(3):90.

PMID: 40025370 DOI: 10.1007/s11274-025-04302-0.

Impact of the elderly lung mucosa on transcriptional adaptation during infection of alveolar epithelial cells.

M Olmo-Fontanez A, Allue-Guardia A, Garcia-Vilanova A, Glenn J, Wang S, Merritt R Microbiol Spectr. 2024; :e0179024.

PMID: 39513699 PMC: 11619525. DOI: 10.1128/spectrum.01790-24.

In Silico Analysis of the Phylogenetic and Physiological Characteristics of Sphingobium indicum B90A: A Hexachlorocyclohexane-Degrading Bacterium.

Kaur J, Verma H, Kaur J, Lata P, Dhingra G, Lal R Curr Microbiol. 2024; 81(8):233.

PMID: 38904756 DOI: 10.1007/s00284-024-03762-1.

Discovery of periplasmic solute binding proteins with specificity for ketone bodies: β-hydroxybutyrate binding proteins.

Kane B, Okuda-Shimazaki J, Andrews M, Kerrigan Jr J, Murphy K, Sode K Protein Sci. 2024; 33(7):e5025.

PMID: 38864689 PMC: 11167705. DOI: 10.1002/pro.5025.

References

Hinsley A, Berks B . Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica. Microbiology (Reading). 2002; 148(Pt 11):3631-3638. DOI: 10.1099/00221287-148-11-3631. View

Olson J, Maier R . Molecular hydrogen as an energy source for Helicobacter pylori. Science. 2002; 298(5599):1788-90. DOI: 10.1126/science.1077123. View

Ray N, Oates J, Turner R, Robinson C . DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus. FEBS Lett. 2003; 534(1-3):156-60. DOI: 10.1016/s0014-5793(02)03839-5. View

Ding Z, Christie P . Agrobacterium tumefaciens twin-arginine-dependent translocation is important for virulence, flagellation, and chemotaxis but not type IV secretion. J Bacteriol. 2003; 185(3):760-71. PMC: 142831. DOI: 10.1128/JB.185.3.760-771.2003. View

Alder N, Theg S . Energetics of protein transport across biological membranes. a study of the thylakoid DeltapH-dependent/cpTat pathway. Cell. 2003; 112(2):231-42. DOI: 10.1016/s0092-8674(03)00032-1. View

Dilks K, Rose R, Hartmann E, Pohlschroder M . Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey. J Bacteriol. 2003; 185(4):1478-83. PMC: 142874. DOI: 10.1128/JB.185.4.1478-1483.2003. View

Finazzi G, Chasen C, Wollman F, de Vitry C . Thylakoid targeting of Tat passenger proteins shows no delta pH dependence in vivo. EMBO J. 2003; 22(4):807-15. PMC: 145441. DOI: 10.1093/emboj/cdg081. View

Sassetti C, Boyd D, Rubin E . Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol. 2003; 48(1):77-84. DOI: 10.1046/j.1365-2958.2003.03425.x. View

Blaudeck N, Kreutzenbeck P, Freudl R, Sprenger G . Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane. J Bacteriol. 2003; 185(9):2811-9. PMC: 154414. DOI: 10.1128/JB.185.9.2811-2819.2003. View

10.

Barrett C, Ray N, Thomas J, Robinson C, Bolhuis A . Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli. Biochem Biophys Res Commun. 2003; 304(2):279-84. DOI: 10.1016/s0006-291x(03)00583-7. View

11.

DeLisa M, Tullman D, Georgiou G . Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc Natl Acad Sci U S A. 2003; 100(10):6115-20. PMC: 156335. DOI: 10.1073/pnas.0937838100. View

12.

Hutcheon G, Bolhuis A . The archaeal twin-arginine translocation pathway. Biochem Soc Trans. 2003; 31(Pt 3):686-9. DOI: 10.1042/bst0310686. View

13.

Bernhardt T, de Boer P . The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol Microbiol. 2003; 48(5):1171-82. PMC: 4428285. DOI: 10.1046/j.1365-2958.2003.03511.x. View

14.

Berks B, Palmer T, Sargent F . The Tat protein translocation pathway and its role in microbial physiology. Adv Microb Physiol. 2003; 47:187-254. DOI: 10.1016/s0065-2911(03)47004-5. View

15.

Dabney-Smith C, Mori H, Cline K . Requirement of a Tha4-conserved transmembrane glutamate in thylakoid Tat translocase assembly revealed by biochemical complementation. J Biol Chem. 2003; 278(44):43027-33. DOI: 10.1074/jbc.M307923200. View

16.

Alami M, Luke I, Deitermann S, Eisner G, Koch H, Brunner J . Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol Cell. 2003; 12(4):937-46. DOI: 10.1016/s1097-2765(03)00398-8. View

17.

DeLisa M, Lee P, Palmer T, Georgiou G . Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. J Bacteriol. 2004; 186(2):366-73. PMC: 305757. DOI: 10.1128/JB.186.2.366-373.2004. View

18.

Schaerlaekens K, Van Mellaert L, Lammertyn E, Geukens N, Anne J . The importance of the Tat-dependent protein secretion pathway in Streptomyces as revealed by phenotypic changes in tat deletion mutants and genome analysis. Microbiology (Reading). 2004; 150(Pt 1):21-31. DOI: 10.1099/mic.0.26684-0. View

19.

Mangels D, Mathers J, Bolhuis A, Robinson C . The core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability. J Mol Biol. 2004; 345(2):415-23. DOI: 10.1016/j.jmb.2004.10.043. View

20.

Jong W, Ten Hagen-Jongman C, Genevaux P, Brunner J, Oudega B, Luirink J . Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in Tat-mediated export. Eur J Biochem. 2004; 271(23-24):4779-87. DOI: 10.1111/j.1432-1033.2004.04442.x. View