The Twin-arginine Translocation Pathway is a Major Route of Protein Export in Streptomyces Coelicolor

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2006 Nov 10

PMID 17093047

Citations 63

Authors

David A Widdick

Kieran Dilks

Govind Chandra

Andrew Bottrill

Mike Naldrett

Mechthild Pohlschroder

Tracy Palmer

Affiliations

Soon will be listed here.

Abstract

The twin-arginine translocation (Tat) pathway is a protein transport system for the export of folded proteins. Substrate proteins are targeted to the Tat translocase by N-terminal signal peptides harboring a distinctive R-R-x-Phi-Phi "twin-arginine" amino acid motif. Using a combination of proteomic techniques, the protein contents from the cell wall of the model Gram-positive bacterium Streptomyces coelicolor were identified and compared with that of mutant strains defective in Tat transport. The proteomic experiments pointed to 43 potentially Tat-dependent extracellular proteins. Of these, 25 were verified as bearing bona fide Tat-targeting signal peptides after independent screening with a facile, rapid, and sensitive reporter assay. The identified Tat substrates, among others, include polymer-degrading enzymes, phosphatases, and binding proteins as well as enzymes involved in secondary metabolism. Moreover, in addition to predicted extracellular substrates, putative lipoproteins were shown to be Tat-dependent. This work provides strong experimental evidence that the Tat system is used as a major general export pathway in Streptomyces.

Citing Articles

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