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Science 18 May 1990:
Vol. 248. no. 4957, pp. 860 - 863
DOI: 10.1126/science.2188362
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Articles
Science, Vol 248, Issue 4957, 860-863
Copyright © 1990 by American Association for the Advancement of Science
No specific recognition of leader peptide by SecB, a chaperone involved in protein export
LL Randall,
TB Topping,
and
SJ Hardy
Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.
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.
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- Exposure of Hydrophobic Surfaces on the Chaperonin GroEL Oligomer by Protonation or Modification of His-401.
- D. L. Gibbons and D. L. Gibbons (1995)
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- Peptide binding by chaperone SecB: implications for recognition of nonnative structure.
- L. Randall (1992)
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257, 241-245
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