Abstract
In the past decade, the interaction between prions and nucleic acids has garnered significant attention from the scientific community. For many years, the participation of RNA and/or DNA in prion pathology has been largely ruled out by the "protein-only" hypothesis, but this is now being reconsidered. Experimental data now indicate that nucleic acids (particularly RNA), besides being carriers of genetic information, function as important key components during development, physiological responsiveness, and cellular signaling. This revelation has brought a new perspective to prion pathology. Here we discuss the role of RNA molecules in prion protein aggregation and the resulting cellular toxicity. We combine our most recent findings with existing literature to shed new light on this exciting field of research.
Acknowledgements
This work was supported by grants from Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Millenium Institute for Structural Biology in Biomedicine and Biotechnology (CNPq Millenium Program), and Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ).
Figures and Tables
Figure 1 Diagram summarizing the findings obtained when rPrP binds either DNA or RNA. While rPrP binds DNA mainly through the C-terminal domain (left), it binds RNA through its N-terminus (right). Small RNAs (SAF9343–59 and opRNA) bind to PrP but only form small, non-toxic oligomeric species in contrast to N2aRNA binding, which forms large oligomers.
![Figure 1 Diagram summarizing the findings obtained when rPrP binds either DNA or RNA. While rPrP binds DNA mainly through the C-terminal domain (left), it binds RNA through its N-terminus (right). Small RNAs (SAF9343–59 and opRNA) bind to PrP but only form small, non-toxic oligomeric species in contrast to N2aRNA binding, which forms large oligomers.](/cms/asset/f0a70e60-8a32-4a3e-961b-5bdaf7459869/kprn_a_10906988_f0001.gif)