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.
Conference Article| February 01 2005
Common principles in the biosynthesis of diverse enzymes
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R.L. Jack, A. Dubini, T. Palmer, F. Sargent; Common principles in the biosynthesis of diverse enzymes. Biochem Soc Trans 1 February 2005; 33 (1): 105–107. doi: https://doi.org/10.1042/BST0330105
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