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Probing structural differences in prion protein isoforms by tyrosine nitration.

Christopher W Lennon1, Holly D Cox, Scott P Hennelly

  • 1Division of Biological Sciences and the Biomolecular Structure and Dynamics Program, The University of Montana, Missoula, Montana 59812, USA.

Biochemistry
|April 3, 2007
PubMed
Summary

Tyrosine nitration reveals structural changes in prion protein. The normal form protects specific tyrosines, which become exposed in the disease-associated beta-oligomeric isoform.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Prion diseases are linked to conformational changes in prion protein (PrP).
  • The normal cellular prion protein (PrP^C) converts to a beta-oligomeric isoform (PrP^Sc), a model for disease-associated fibrils.
  • Understanding these structural transitions is crucial for disease mechanism research.

Purpose of the Study:

  • To investigate conformational differences between PrP^C and its disease-associated isoform using chemical labeling.
  • To identify specific regions of the prion protein that change their chemical environment during conversion.

Main Methods:

  • Recombinant hamster prion protein (residues 90-232) was used.
  • Two conformational isomers were probed using tyrosine nitration with peroxynitrite and tetranitromethane.

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  • Changes in tyrosine reactivity were monitored to infer structural alterations.

    • Main Results:

    • Two conserved tyrosines (149 and 150) were unreactive in PrP^C but became reactive in the beta-oligomeric isoform.
    • Two other tyrosines (225 and 226) showed decreased reactivity after conversion to the beta-oligomeric form.
    • These findings indicate distinct chemical environments for specific tyrosines in different prion protein conformations.

    Conclusions:

    • Tyrosine nitration effectively distinguishes between prion protein conformational states.
    • Specific tyrosine residues undergo significant environmental changes upon conversion to the beta-oligomeric structure.
    • This method aids in characterizing the structural basis of prion protein misfolding and disease.