Export of complex cofactor-containing proteins by the bacterial Tat pathway

Tracy Palmer, Frank Sargent, Ben C. Berks

    Research output: Contribution to journalArticle

    163 Citations (Scopus)

    Abstract

    The twin-arginine (Tat) protein translocase is a highly unusual protein transport machine that is dedicated to the movement of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat pathway by means of N-terminal signal peptides harbouring a distinctive twin-arginine motif. In the model organism Escherichia coli, many of the Tat substrates bind redox cofactors that are inserted into apo-proteins before they engage with the Tat machinery. Here we review recent advances in understanding the events involved in the coordination of cofactor insertion with the export process. Current models for Tat protein transport are also discussed.

    Original languageEnglish
    Pages (from-to)175-180
    Number of pages6
    JournalTrends in Microbiology
    Volume13
    Issue number4
    DOIs
    Publication statusPublished - 2005

    Cite this

    Palmer, Tracy ; Sargent, Frank ; Berks, Ben C. / Export of complex cofactor-containing proteins by the bacterial Tat pathway. In: Trends in Microbiology. 2005 ; Vol. 13, No. 4. pp. 175-180.
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    Export of complex cofactor-containing proteins by the bacterial Tat pathway. / Palmer, Tracy; Sargent, Frank; Berks, Ben C.

    In: Trends in Microbiology, Vol. 13, No. 4, 2005, p. 175-180.

    Research output: Contribution to journalArticle

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    AU - Sargent, Frank

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