The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor

David A. Widdick, Kieran Dilks, Govind Chandra, Andrew Bottrill, Mike Naldrett, Mechthild Pohlschröder, Tracy Palmer

Research output: Contribution to journalArticlepeer-review

112 Scopus citations


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-Φ-Φ "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 polymerdegrading 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.

Original languageEnglish (US)
Pages (from-to)17927-17932
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number47
StatePublished - Nov 21 2006
Externally publishedYes


  • Protein transport
  • Proteome
  • Secondary metabolism
  • Tat pathway
  • Twin arginine signal peptide

ASJC Scopus subject areas

  • General


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