RNA-seq analyses reveal the relevance of RNAs involved in ribosomal complex to induce mammalian prion protein aggregation and phase separation <i>in vitro</i>.

ABSTRACT: Conformational conversion of cellular prion protein (PrP^C) into infectious PrP (PrP^Sc) is one of the most intriguing processes in modern Biology. It is well accepted that this transition is catalysed by one or more cofactors that lower the energy barrier between the different PrP forms. Among potential candidates, RNA molecules are strong contenders. Our group has pursued nucleic acids, both DNA and RNA, capable of inducing PrP misfolding, aggregation, and, more recently, phase separation, a process proposed to precede aggregation in degenerative disorders. We found that the interaction between recombinant PrP (rPrP) and total RNA extracted from neuroblastoma cells (N2aRNA) results in significant structural alterations. Here, we use rPrP:N2aRNA as a model to search fo

SUBMITTER: Tahira AC 

PROVIDER: S-EPMC12123958 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature