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

David Widdick, Kieran Dilks, Govind Chandra, Andrew Bottrill, Mike Naldrett, Mechthild Pohlschroder, Tracy Palmer, Jonathan Beckwith (Editor)

    Research output: Contribution to journalArticlepeer-review

    111 Citations (Scopus)

    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-F-F “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.
    Original languageEnglish
    Pages (from-to)17927-17932
    Number of pages6
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume103
    Issue number47
    DOIs
    Publication statusPublished - 2006

    Keywords

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

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