Coordinating Assembly and Export of Complex Bacterial Proteins

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 2004 Sep 24

PMID 15385959

Citations 78

Authors

Rachael L Jack

Grant Buchanan

Alexandra Dubini

Kostas Hatzixanthis

Tracy Palmer

Frank Sargent

Affiliations

Soon will be listed here.

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.

Citing Articles

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Highly efficient export of a disulfide-bonded protein to the periplasm and medium by the Tat pathway using CyDisCo in Escherichia coli.

Arauzo-Aguilera K, Saaranen M, Robinson C, Ruddock L Microbiologyopen. 2023; 12(2):e1350.

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Analysis of the Brucella suis Twin Arginine Translocation System and Its Substrates Shows That It Is Essential for Viability.

Riquelme E, Omarova S, Ize B, OCallaghan D Infect Immun. 2022; 91(1):e0045922.

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