Common principles in the biosynthesis of diverse enzymes.
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.
Jack
R L
RL
School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, England, UK.
Dubini
A
A
Palmer
T
T
Sargent
F
F
D004798:Enzymes / Q000096:biosynthesis*; D029968:Escherichia coli Proteins / Q000096:biosynthesis / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000096:biosynthesis; D018832:Molecular Chaperones / Q000378:metabolism
D004798:Enzymes; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones; C088083:TorD protein, E coli; C408585:twin-arginine translocase complex, E coli