Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates.
Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones, redox enzyme maturation proteins (REMPs). Here various regions of the RR-containing oxidoreductase subunit (leader peptide, full preprotein with and without a leader cleavage site, mature protein) were assayed for interaction with their REMPs. All REMPs bound their preprotein substrates independent of the cleavage site. Some showed binding to either the leader or mature region, whereas in one case only the preprotein bound its REMP. The absence of Tat also influenced the amount of chaperone-substrate interaction.
Department of Biological Sciences, Faculty of Science, University of Calgary, Calgary, Alberta, Canada.
Catherine S
CS
Chan
Limei
L
Chang
Tara M L
TM
Winstone
Raymond J
RJ
Turner
D020816:Amino Acid Motifs; D001120:Arginine; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones; D021122:Protein Subunits; C408585:twin-arginine translocase complex, E coli; D001120:Arginine; D010088:Oxidoreductases