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No specific recognition of leader peptide by SecB, a chaperone involved in protein export
L L Randall1, T B Topping, S J Hardy
1Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.
Science (New York, N.Y.)
|May 18, 1990
Abstract:
Most proteins destined for export from Escherichia coli are made as precursors containing amino-terminal leader sequences that are essential for export and that are removed during the process. The initial step in export of a subset of proteins, which includes maltose-binding protein, is binding of the precursor by the molecular chaperone SecB. This work shows directly that SecB binds with high affinity to unfolded maltose-binding protein but does not specifically recognize and bind the leader. Rather, the leader modulates folding to expose elements in the remainder of the polypeptide that are recognized by SecB.