Signal peptide-chaperone interactions on the twin-arginine protein transport pathway

Hatzixanthis, Kostas, Clarke, Thomas A., Oubrie, Arthur, Richardson, David J., Turner, Raymond J. and Sargent, Frank (2005) Signal peptide-chaperone interactions on the twin-arginine protein transport pathway. Proceedings of the National Academy of Sciences, 102. pp. 8460-8465. ISSN 0027-8424

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Abstract

The twin-arginine transport (Tat) system is a protein-targeting pathway of prokaryotes and chloroplasts. Most Escherichia coli Tat substrates are complex metalloenzymes that must be correctly folded and assembled before transport, and a preexport chaperone-mediated “proofreading” process is therefore in operation. The paradigm proofreading chaperone is TorD, which coordinates maturation and export of the key respiratory enzyme trimethylamine N-oxide reductase (TorA). It is demonstrated here that purified TorD binds tightly and with exquisite specificity to the TorA twin-arginine signal peptide in vitro. It is also reported that the TorD family constitutes a hitherto unexpected class of nucleotide-binding proteins. The affinity of TorD for GTP is enhanced by initial signal peptide binding, and it is proposed that GTP governs signal peptide binding-and-release cycles during Tat proofreading.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Depositing User: EPrints Services
Date Deposited: 01 Oct 2010 13:37
Last Modified: 21 Apr 2020 19:56
URI: https://ueaeprints.uea.ac.uk/id/eprint/1020
DOI: 10.1073/pnas.0500737102

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