A regulatory domain controls the transport activity of a twin-arginine signal peptide

Lisa Bowman, Tracy Palmer, Frank Sargent (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    4 Citations (Scopus)

    Abstract

    The twin-arginine translocation (Tat) pathway is used by bacteria for the transmembrane transport of folded proteins. Proteins are targeted to the Tat translocase by signal peptides that have common tripartite structures consisting of polar n-regions, hydrophobic h-regions, and polar c-regions. In this work, the signal peptide of [NiFe] hydrogenase-1 from Escherichia coli has been studied. The hydrogenase-1 signal peptide contains an extended n-region that has a conserved primary structure. Genetic and biochemical approaches reveal that the signal peptide n-region is essential for hydrogenase assembly and acts as a regulatory domain controlling transport activity of the signal peptide.
    Original languageEnglish
    Pages (from-to)3365-3370
    Number of pages6
    JournalFEBS Letters
    Volume587
    Issue number20
    DOIs
    Publication statusPublished - 11 Oct 2013

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