Reports

No specific recognition of leader peptide by SecB, a chaperone involved in protein export

Science  18 May 1990:
Vol. 248, Issue 4957, pp. 860-863
DOI: 10.1126/science.2188362

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.

Related Content