The "Jekyll and Hyde" Actions of Nucleic Acids on the Prion-like Aggregation of Proteins.
Protein misfolding results in devastating degenerative diseases and cancer. Among the culprits involved in these illnesses are prions and prion-like proteins, which can propagate by converting normal proteins to the wrong conformation. For spongiform encephalopathies, a real prion can be transmitted among individuals. In other disorders, the bona fide prion characteristics are still under investigation. Besides inducing misfolding of native proteins, prions bind nucleic acids and other polyanions. Here, we discuss how nucleic acid binding might influence protein misfolding for both disease-related and benign, functional prions and why the line between bad and good amyloids might be more subtle than previously thought.
From the Programa de Biologia Estrutural, Instituto de Bioquímica Médica Leopoldo de Meis, Instituto Nacional de Biologia Estrutural e Bioimagem, Centro Nacional de Ressonância Magnética Nuclear Jiri Jonas, and jerson@bioqmed.ufrj.br.
Jerson L
JL
Silva
the Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
Yraima
Y
Cordeiro
D000818:Animals; D006801:Humans; D009696:Nucleic Acids / Q000378:metabolism*; D011328:Prions / Q000378:metabolism*; D066263:Protein Aggregation, Pathological / Q000378:metabolism*
D009696:Nucleic Acids; D011328:Prions
cancer; functional amyloid; functional amyloids; neurodegenerative disease; nucleic acid; p53; prion; prions; protein aggregation; protein misfolding