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Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence

Yukihiro Yabuta1, Ezhilkani Subbian, Catherine Oiry

  • 1Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, Oregon 97239-3098, USA.

The Journal of Biological Chemistry
|February 13, 2003
PubMed
Summary

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This study redesigned a subtilisin peptide chaperone (propeptide) to identify minimum sequence requirements for function. The novel propeptide (ProD) effectively guided folding and inhibited subtilisin, demonstrating conserved scaffolds, not charge, dictate function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Folding

Background:

  • Protease catalytic domains require N-terminal propeptides (intramolecular chaperones) for proper folding.
  • Propeptides are less conserved, charged, and show low inter-family similarity, leaving functional requirements unclear.

Purpose of the Study:

  • To determine the minimum sequence requirements for a functional subtilisin propeptide.
  • To design novel, tailor-made peptide chaperones.

Main Methods:

  • Utilized a decision-based computer algorithm on multiple sequence alignments to redesign the subtilisin propeptide.
  • Designed a novel peptide sequence (ProD) by varying non-conserved residues while maintaining conserved ones.

Main Results:

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  • The redesigned ProD exhibited 16% sequence identity and a 5 pH unit difference from the wild-type (ProWT) but effectively chaperoned folding and inhibited subtilisin.
  • ProD and ProWT showed similar computed secondary structures and hydrophobic patterns.
  • ProD formed a stoichiometric complex with mature subtilisin, with similar CD spectra to the ProWT-subtilisin complex.

Conclusions:

  • Conserved structural scaffolds and hydrophobic patterns, rather than absolute charge distribution, are critical for propeptide function.
  • This finding facilitates the design of specific peptide chaperones for protease families.