Common principles in the biosynthesis of diverse enzymes

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

    Research output: Contribution to journalArticlepeer-review

    9 Citations (Scopus)


    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
    Issue number1
    Publication statusPublished - 2005
    Event7th International Hydrogenases Conference - Reading, United Kingdom
    Duration: 24 Aug 200429 Aug 2004


    Dive into the research topics of 'Common principles in the biosynthesis of diverse enzymes'. Together they form a unique fingerprint.

    Cite this