Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone

Buchanan, Grant, Maillard, Julien, Nabuurs, Sander B., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Palmer, Tracy and Sargent, Frank (2008) Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone. FEBS Letters, 582 (29). pp. 3979-3984. ISSN 1873-3468

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Abstract

The twin-arginine translocation (Tat) system is a bacterial protein targeting pathway. Tat-targeted proteins display signal peptides containing a distinctive SRRxFLK ‘twin-arginine’ motif. The Escherichia coli trimethylamine N-oxide reductase (TorA) bears a bifunctional Tat signal peptide, which directs protein export and serves as a binding site for the TorD biosynthetic chaperone. Here, the physical interaction between TorD and the TorA signal peptide was investigated. A single substitution within the TorA signal peptide (L31Q) was sufficient to impair TorD binding. Screening of a random torD mutant library identified a variant TorD protein (Q7L) that displayed increased binding affinity for the TorA signal peptide.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Depositing User:	EPrints Services
Date Deposited:	01 Oct 2010 13:36
Last Modified:	24 Sep 2024 09:27
URI:	https://ueaeprints.uea.ac.uk/id/eprint/175
DOI:	10.1016/j.febslet.2008.10.049

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