Assembly of membrane-bound respiratory complexes by the Tat protein-transport system

Frank Sargent, Ben C Berks, Tracy Palmer

    Research output: Contribution to journalReview article

    79 Citations (Scopus)

    Abstract

    The Tat protein-export system serves to translocate folded proteins, often containing redox cofactors, across the bacterial inner membrane. Substrate proteins are directed to the Tat apparatus by distinctive N-terminal signal peptides containing a consensus SRRxFLK "twin-arginine" motif. Here we review recent studies of the Tat system with particular emphasis on the assembly of membrane-bound respiratory complexes. We discuss the connection between Tat targeting and topological organisation of the complexes and consider the role of chaperone proteins in cofactor insertion and Tat targeting. The crystal structure of Escherichia coli formate dehydrogenase-N demonstrates that some Tat substrates are integral membrane proteins. Sequence analysis suggests that one-quarter of all traffic on the E. coli Tat pathway is inner-membrane proteins.

    Original languageEnglish
    Pages (from-to)77-84
    Number of pages8
    JournalArchives of Microbiology
    Volume178
    Issue number2
    DOIs
    Publication statusPublished - Aug 2002

    Cite this

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    title = "Assembly of membrane-bound respiratory complexes by the Tat protein-transport system",
    abstract = "The Tat protein-export system serves to translocate folded proteins, often containing redox cofactors, across the bacterial inner membrane. Substrate proteins are directed to the Tat apparatus by distinctive N-terminal signal peptides containing a consensus SRRxFLK {"}twin-arginine{"} motif. Here we review recent studies of the Tat system with particular emphasis on the assembly of membrane-bound respiratory complexes. We discuss the connection between Tat targeting and topological organisation of the complexes and consider the role of chaperone proteins in cofactor insertion and Tat targeting. The crystal structure of Escherichia coli formate dehydrogenase-N demonstrates that some Tat substrates are integral membrane proteins. Sequence analysis suggests that one-quarter of all traffic on the E. coli Tat pathway is inner-membrane proteins.",
    author = "Frank Sargent and Berks, {Ben C} and Tracy Palmer",
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    Assembly of membrane-bound respiratory complexes by the Tat protein-transport system. / Sargent, Frank; Berks, Ben C ; Palmer, Tracy.

    In: Archives of Microbiology, Vol. 178, No. 2, 08.2002, p. 77-84.

    Research output: Contribution to journalReview article

    TY - JOUR

    T1 - Assembly of membrane-bound respiratory complexes by the Tat protein-transport system

    AU - Sargent, Frank

    AU - Berks, Ben C

    AU - Palmer, Tracy

    PY - 2002/8

    Y1 - 2002/8

    N2 - The Tat protein-export system serves to translocate folded proteins, often containing redox cofactors, across the bacterial inner membrane. Substrate proteins are directed to the Tat apparatus by distinctive N-terminal signal peptides containing a consensus SRRxFLK "twin-arginine" motif. Here we review recent studies of the Tat system with particular emphasis on the assembly of membrane-bound respiratory complexes. We discuss the connection between Tat targeting and topological organisation of the complexes and consider the role of chaperone proteins in cofactor insertion and Tat targeting. The crystal structure of Escherichia coli formate dehydrogenase-N demonstrates that some Tat substrates are integral membrane proteins. Sequence analysis suggests that one-quarter of all traffic on the E. coli Tat pathway is inner-membrane proteins.

    AB - The Tat protein-export system serves to translocate folded proteins, often containing redox cofactors, across the bacterial inner membrane. Substrate proteins are directed to the Tat apparatus by distinctive N-terminal signal peptides containing a consensus SRRxFLK "twin-arginine" motif. Here we review recent studies of the Tat system with particular emphasis on the assembly of membrane-bound respiratory complexes. We discuss the connection between Tat targeting and topological organisation of the complexes and consider the role of chaperone proteins in cofactor insertion and Tat targeting. The crystal structure of Escherichia coli formate dehydrogenase-N demonstrates that some Tat substrates are integral membrane proteins. Sequence analysis suggests that one-quarter of all traffic on the E. coli Tat pathway is inner-membrane proteins.

    U2 - 10.1007/s00203-002-0434-2

    DO - 10.1007/s00203-002-0434-2

    M3 - Review article

    VL - 178

    SP - 77

    EP - 84

    JO - Archives of Microbiology

    JF - Archives of Microbiology

    SN - 0302-8933

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    ER -