Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.
Publication year
2008Source
FEBS Letters, 582, 29, (2008), pp. 3979-84ISSN
Publication type
Article / Letter to editor
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Organization
CMBI
Former Organization
Bioinformatics (umcn)
Journal title
FEBS Letters
Volume
vol. 582
Issue
iss. 29
Page start
p. 3979
Page end
p. 84
Subject
NCMLS 3: Growth and differentiationAbstract
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.
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- Academic publications [245011]
- Faculty of Medical Sciences [93198]
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