Open AccessDemonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning
Author(s) -
Vijaya J. Khisty,
Linda L. Randall
Publication year - 1995
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.177.11.3277-3282.1995
Subject(s) - maltose binding protein , maltose , biology , biochemistry , periplasmic space , plasma protein binding , biophysics , binding site , binding protein , chaperone (clinical) , enzyme , fusion protein , escherichia coli , recombinant dna , medicine , pathology , gene
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.