Common principles in the biosynthesis of diverse enzymes
Common principles in the biosynthesis of diverse enzymes
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DOI:
10.1042/bst0330105
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发表时间:
2005-02-01
影响因子:
3.9
通讯作者:
Sargent, F
中科院分区:
文献类型:
--
作者:
Jack, RL;Dubini, A;Sargent, F
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.