Silva Jerson L, Cordeiro Yraima
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
the Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
J Biol Chem. 2016 Jul 22;291(30):15482-90. doi: 10.1074/jbc.R116.733428. Epub 2016 Jun 10.
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.
蛋白质错误折叠会导致毁灭性的退行性疾病和癌症。引发这些疾病的罪魁祸首包括朊病毒和类朊病毒蛋白,它们可通过将正常蛋白质转变为错误构象来进行传播。对于海绵状脑病而言,真正的朊病毒能够在个体之间传播。在其他病症中,真正的朊病毒特征仍在研究之中。除了诱导天然蛋白质错误折叠外,朊病毒还能结合核酸和其他聚阴离子。在此我们将探讨核酸结合如何影响与疾病相关的以及良性功能性朊病毒的蛋白质错误折叠,以及为何有害与有益淀粉样蛋白之间的界限可能比之前认为的更为微妙。