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Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone |
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| Authors: | Grant Buchanan Sander B Nabuurs Tracy Palmer |
| Institution: | a Division of Molecular and Environmental Microbiology, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, United Kingdom b School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, England, United Kingdom c Centre for Molecular and Biomolecular Informatics, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen, P.O. Box 9010, 6500 GL Nijmegen, The Netherlands |
| 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.Structured summary
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| Keywords: | Tat twin-arginine translocation TMAO trimethylamine N-oxide |
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