Effect of enzymatic deimination on the conformation of recombinant prion protein

Young, Duncan S., Meersman, Filip, Oxley, David , Webster, Judith, Gill, Andrew C., Bronstein, Igor, 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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