Intriguing nucleic-acid-binding features of mammalian prion protein.
In transmissible spongiform encephalopathies, the infectious material consists chiefly of a protein, the scrapie prion protein PrP(Sc), that carries no genetic coding material; however, prions are likely to have accomplices that chaperone their activity and promote the conversion of the cellular prion protein PrP(C) into the disease-causing isoform (PrP(Sc)). Recent studies from several laboratories indicate that PrP(C) recognizes many nucleic acids (NAs) with high affinities, and we correlate these findings with a possible pathophysiological role for this interaction. Thus, of the chaperones, NA is the most likely candidate for prions. The participation of NAs in prion propagation opens new avenues for developing new diagnostic tools and therapeutics to target prion diseases, as well as for understanding the function of PrP(C), probably as a NA chaperone.
Silva
Jerson L
JL
Instituto de Bioquímica Médica, Centro Nacional de Ressonância Magnética Nuclear Jiri Jonas, Universidade Federal do Rio de Janeiro, RJ 21941-590, Rio de Janeiro, Brazil. jerson@bioqmed.ufrj.br
Lima
Luís Maurício T R
LM
Foguel
Debora
D
Cordeiro
Yraima
Y
D000818:Animals; D006801:Humans; D008954:Models, Biological; D009696:Nucleic Acids / Q000378:metabolism*; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation
D009696:Nucleic Acids; D011328:Prions