Export of complex cofactor-containing proteins by the bacterial Tat pathway.
The twin-arginine (Tat) protein translocase is a highly unusual protein transport machine that is dedicated to the movement of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat pathway by means of N-terminal signal peptides harbouring a distinctive twin-arginine motif. In the model organism Escherichia coli, many of the Tat substrates bind redox cofactors that are inserted into apo-proteins before they engage with the Tat machinery. Here we review recent advances in understanding the events involved in the coordination of cofactor insertion with the export process. Current models for Tat protein transport are also discussed.
Palmer
Tracy
T
Department of Molecular Microbiology, John Innes Centre, Norwich, UK NR4 7UH. tracy.palmer@bbsrc.edu
Sargent
Frank
F
Berks
Ben C
BC
D001419:Bacteria / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D003067:Coenzymes / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism*; D008954:Models, Biological; D017510:Protein Folding; D021381:Protein Transport / Q000235:genetics
D001426:Bacterial Proteins; D003067:Coenzymes; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; C408585:twin-arginine translocase complex, E coli