Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning.
An early step in the export of maltose-binding protein to the periplasm is interaction with the molecular chaperone SecB. We demonstrate that binding to SecB in vivo is determined by a kinetic partitioning between the folding of maltose-binding protein to its native state and its association with SecB. A complex of SecB and a species of maltose-binding protein that folds slowly is shown to be longer-lived than a complex of the wild-type maltose-binding protein and SecB. In addition, we show that incomplete nascent chains, which are unable to fold, remain complexed with SecB.
Khisty
V J
VJ
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.
Randall
L L
LL
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002451:Cell Compartmentation; D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D018832:Molecular Chaperones / Q000378:metabolism*; D009004:Monosaccharide Transport Proteins; D011485:Protein Binding; D017510:Protein Folding
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D018832:Molecular Chaperones; D009004:Monosaccharide Transport Proteins; C057842:SecB protein, Bacteria; C461599:maltose transport system, E coli