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Article

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

FEBS letters - 10 Dec 2008

Buchanan Grant, Maillard Julien, Nabuurs Sander B, Richardson David J, Palmer Tracy, Sargent Frank

Abstract excerpt

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...

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Source

Identifiers

PMID: 19013157
DOI: 10.1016/j.febslet.2008.10.049

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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