Effect of enzymatic deimination on the conformation of recombinant prion protein

Young, Duncan S. and Meersman, Filip and Oxley, David and Webster, Judith and Gill, Andrew C. and Bronstein, Igor and Lowe, Christopher R. and Dear, Denise V. (2009) Effect of enzymatic deimination on the conformation of recombinant prion protein. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1794 (8). pp. 1123-1133. ISSN 1570-9639

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Abstract

Deimination is the post-translational conversion of arginine residues to citrulline. It has been implicated as a causative factor in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis and more recently, as a marker of neurodegeneration. We have investigated the effect of the post-translational modification of arginine residues on the structure of recombinant ovine prion protein. Deiminated prion protein exhibited biophysical properties characteristic of the scrapie-associated conformer of prion protein viz. an increased β-sheet secondary structure, congophilic structures indicative of amyloid and proteinase K resistance which could be templated onto normal unmodified prion protein. In the light of these findings, a potential role of post-translational modifications to prion protein in disease initiation or propagation is discussed.

Keywords:prion, post-translational modification, conformational change, deimination, citrulline, arginine modification, amyloid
Subjects:C Biological Sciences > C770 Biophysical Science
C Biological Sciences > C760 Biomolecular Science
Divisions:College of Science
ID Code:29482
Deposited On:16 Mar 2018 15:09

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