Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli.
Sensitivity to proteolytic degradation was used to monitor folding of polypeptides in vivo. A correlation between competence for export and lack of stable tertiary structure was established by comparing the kinetics of folding of mutated precursor maltose-binding protein that carries a defective leader peptide with the kinetics of folding of wild-type precursor that is competent for export. It is proposed that during export a kinetic competition exists between productive translocation and folding of precursor intracellularly into a stable conformation that is not compatible with transfer.
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D002451:Cell Compartmentation; D019286:Endopeptidase K; D010450:Endopeptidases; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D007700:Kinetics; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins / Q000378:metabolism*; D009004:Monosaccharide Transport Proteins; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D013329:Structure-Activity Relationship
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins; D009004:Monosaccharide Transport Proteins; C461599:maltose transport system, E coli; D010450:Endopeptidases; D019286:Endopeptidase K