Sequence analysis of bacterial redox enzyme maturation proteins (REMPs).
The twin-arginine protein transport (Tat) system is a remarkable molecular machine dedicated to the translocation of fully folded proteins across energy-transducing membranes. Complex cofactor-containing Tat substrates acquire their cofactors prior to export, and substrate proteins actually require to be folded before transport can proceed. Thus, it is very likely that mechanisms exist to prevent wasteful export of immature Tat substrates or to curb competition between immature and mature substrates for the transporter. Here we assess the primary sequence relationships between the accessory proteins implicated in this process during assembly of key respiratory enzymes in the model prokaryote Escherichia coli. For each respiratory enzyme studied, a redox enzyme maturation protein (REMP) was assigned. The main finding from this review was the hitherto unexpected link between the Tat-linked REMP DmsD and the nitrate reductase biosynthetic protein NarJ. The evolutionary link between Tat transport and cofactor insertion processes is discussed.
Turner
Raymond J
RJ
Department of Biological Sciences, University of Calgary, Alberta, Canada. turnerr@ucalgary.edu
Papish
Andriyka L
AL
Sargent
Frank
F
D001419:Bacteria / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000145:classification* / Q000235:genetics / Q000378:metabolism; D001692:Biological Transport; D002352:Carrier Proteins / Q000134:cerebrospinal fluid* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000134:cerebrospinal fluid* / Q000235:genetics; D047908:Intracellular Signaling Peptides and Proteins; D026901:Membrane Transport Proteins / Q000145:classification / Q000235:genetics
D001426:Bacterial Proteins; D002352:Carrier Proteins; C434268:DmsD protein, E coli; D029968:Escherichia coli Proteins; D047908:Intracellular Signaling Peptides and Proteins; D026901:Membrane Transport Proteins