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Science 10 July 1992:
Vol. 257. no. 5067, pp. 241 - 245
DOI: 10.1126/science.1631545
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Articles
Science, Vol 257, Issue 5067, 241-245
Copyright © 1992 by American Association for the Advancement of Science
Peptide binding by chaperone SecB: implications for recognition of nonnative structure
LL Randall
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.
The molecular basis for recognition of nonnative proteins by the molecular chaperone SecB was investigated with an in vitro assay based on the protection of SecB from proteolysis when a ligand is bound. The SecB tetramer has multiple binding sites for positively charged peptides. When the peptide binding sites are occupied, the complex undergoes a conformational change to expose hydrophobic sites that bind the fluorescent probe 1-anilinonaphthalene-8-sulfonate. A model is proposed for interaction of nonnative polypeptides with both hydrophilic and hydrophobic sites on SecB.
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