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Peptide binding by chaperone SecB: implications for recognition of nonnative structure.

L L Randall1

  • 1Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.

Science (New York, N.Y.)
|July 10, 1992
PubMed
Summary

The molecular chaperone SecB recognizes nonnative proteins through distinct binding sites. Ligand binding induces conformational changes, exposing new sites for further interactions, crucial for protein folding.

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Area of Science:

  • Molecular biology
  • Protein folding
  • Biochemistry

Background:

  • Molecular chaperones are essential for protein homeostasis.
  • SecB is a key chaperone involved in protein translocation and folding.
  • Understanding SecB's recognition mechanism is vital for protein folding studies.

Purpose of the Study:

  • To investigate the molecular basis of nonnative protein recognition by the SecB chaperone.
  • To elucidate the binding sites and conformational changes involved in SecB-ligand interactions.

Main Methods:

  • Utilized an in vitro proteolysis protection assay to monitor SecB-ligand binding.
  • Employed a fluorescent probe (1-anilinonaphthalene-8-sulfonate) to detect conformational changes.
  • Characterized binding sites for positively charged peptides on the SecB tetramer.

Main Results:

  • SecB possesses multiple binding sites for positively charged peptides.
  • Ligand binding to these sites induces a conformational change in SecB.
  • This conformational change exposes hydrophobic sites, which can bind to fluorescent probes.

Conclusions:

  • A model for SecB's interaction with nonnative polypeptides is proposed.
  • SecB recognizes nonnative proteins via both hydrophilic and hydrophobic interactions.
  • These interactions are critical for SecB's chaperone function in protein folding.