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

Full text not available from this repository. (Request a copy)

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:	17 Sep 2020 23:43
URI:	https://ueaeprints.uea.ac.uk/id/eprint/1020
DOI:	10.1073/pnas.0500737102

Actions (login required)

View Item