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Related Experiment Videos

Substrate specificity of the SecB chaperone.

N T Knoblauch1, S Rüdiger, H J Schönfeld

  • 1Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany.

The Journal of Biological Chemistry
|November 24, 1999
PubMed
Summary
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Bacterial chaperone SecB binds proteins via a motif rich in aromatic and basic residues. This chaperone lacks specificity for signal sequences, suggesting a general role in protein translocation.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Folding

Background:

  • The bacterial chaperone SecB facilitates protein translocation across the inner membrane.
  • The precise mechanism by which SecB distinguishes between secretory and cytosolic proteins remains unclear.

Purpose of the Study:

  • To identify the specific binding motif of SecB.
  • To determine if SecB exhibits specificity towards signal sequences or different protein classes.

Main Methods:

  • Screening of 2688 peptides from 23 proteins to identify SecB binding.
  • Sequence analysis to define the SecB binding motif.
  • Prediction of SecB binding regions in protein sequences.

Main Results:

Related Experiment Videos

  • A 9-residue motif enriched in aromatic and basic residues, disfavoring acidic residues, was identified for SecB binding.
  • SecB binding regions occur every 20-30 residues and show similar affinity in various protein types.
  • SecB demonstrated a lack of specificity for signal sequences and bound denatured proteins.

    • Conclusions:

    • SecB's binding specificity does not differentiate between secretory and non-secretory proteins.
    • SecB functions as a general chaperone, with translocation involvement mediated by interactions with the translocation apparatus.