Common principles in the biosynthesis of diverse enzymes

R. L. Jack, A. Dubini, T. Palmer, F. Sargent

    Research output: Contribution to journalArticle

    9 Citations (Scopus)

    Abstract

    A subset of bacterial periplasmic enzymes are transported from the cytoplasm by the twin-arginine transport apparatus. Such proteins contain distinctive N-terminal signal peptides containing a conserved SRRXFLK 'twin-arginine' amino acid motif and often bind complex cofactors before the transport event. It is important that assembly of complex cofactor-containing, and often multi-subunit, enzymes is complete before export. Studies of the unrelated [NiFe] hydrogenase, DMSO reductase and trimethylamine N-oxide reductase systems from Escherichia coli have enabled us to define a chaperone-mediated 'proofreading' mechanism involved in co-ordinating assembly and export of twin-arginine transport-dependent enzymes.

    Original languageEnglish
    Pages (from-to)105-107
    Number of pages3
    JournalBiochemical Society Transactions
    Volume33
    Issue number1
    Publication statusPublished - 2005
    Event7th International Hydrogenases Conference - Reading, United Kingdom
    Duration: 24 Aug 200429 Aug 2004

    Cite this

    Jack, R. L., Dubini, A., Palmer, T., & Sargent, F. (2005). Common principles in the biosynthesis of diverse enzymes. Biochemical Society Transactions, 33(1), 105-107.
    Jack, R. L. ; Dubini, A. ; Palmer, T. ; Sargent, F. . / Common principles in the biosynthesis of diverse enzymes. In: Biochemical Society Transactions. 2005 ; Vol. 33, No. 1. pp. 105-107.
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    Jack, RL, Dubini, A, Palmer, T & Sargent, F 2005, 'Common principles in the biosynthesis of diverse enzymes', Biochemical Society Transactions, vol. 33, no. 1, pp. 105-107.

    Common principles in the biosynthesis of diverse enzymes. / Jack, R. L. ; Dubini, A. ; Palmer, T. ; Sargent, F. .

    In: Biochemical Society Transactions, Vol. 33, No. 1, 2005, p. 105-107.

    Research output: Contribution to journalArticle

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    AU - Jack, R. L.

    AU - Dubini, A.

    AU - Palmer, T.

    AU - Sargent, F.

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    N2 - A subset of bacterial periplasmic enzymes are transported from the cytoplasm by the twin-arginine transport apparatus. Such proteins contain distinctive N-terminal signal peptides containing a conserved SRRXFLK 'twin-arginine' amino acid motif and often bind complex cofactors before the transport event. It is important that assembly of complex cofactor-containing, and often multi-subunit, enzymes is complete before export. Studies of the unrelated [NiFe] hydrogenase, DMSO reductase and trimethylamine N-oxide reductase systems from Escherichia coli have enabled us to define a chaperone-mediated 'proofreading' mechanism involved in co-ordinating assembly and export of twin-arginine transport-dependent enzymes.

    AB - A subset of bacterial periplasmic enzymes are transported from the cytoplasm by the twin-arginine transport apparatus. Such proteins contain distinctive N-terminal signal peptides containing a conserved SRRXFLK 'twin-arginine' amino acid motif and often bind complex cofactors before the transport event. It is important that assembly of complex cofactor-containing, and often multi-subunit, enzymes is complete before export. Studies of the unrelated [NiFe] hydrogenase, DMSO reductase and trimethylamine N-oxide reductase systems from Escherichia coli have enabled us to define a chaperone-mediated 'proofreading' mechanism involved in co-ordinating assembly and export of twin-arginine transport-dependent enzymes.

    M3 - Article

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    JO - Biochemical Society Transactions

    JF - Biochemical Society Transactions

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