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Hatzixanthis, Kostas, Clarke, Thomas A. 
ORCID: https://orcid.org/0000-0002-6234-1914, Oubrie, Arthur, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, 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
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: | 22 Dec 2022 06:33 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/1020 |
| DOI: | 10.1073/pnas.0500737102 |
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