Abstract

The role of the nucleic acids in prion aggregation/disaggregation is becoming more and more evident. Here, using HET-s prion from fungiPodospora anserina(P. anserina) as a model system, we studied the role of RNA, particularly of different domains of the ribosomal RNA (rRNA), in its aggregation process. Our results using Rayleigh light scattering, Thioflavin T (ThT) binding, transmission electron microscopy (TEM) and cross-seeding assay show that rRNA, in particular the domain V of the major rRNA from the large subunit of the ribosome, substantially prevents insoluble amyloid and amorphous aggregation of the HET-s prion in a concentration-dependent manner. Instead, it facilitates the formation of the soluble oligomeric "seeds", which are capable of promoting de novo HET-s aggregation. The sites of interactions of the HET-s prion protein on domain V rRNA were identified by primer extension analysis followed by UV-crosslinking, which overlap with the sites previously identified for the protein-folding activity of the ribosome (PFAR). This study clarifies a missing link between the rRNA-based PFAR and the mode of propagation of the fungal prions.

Keywords

ribosomal RNA; prion aggregation; P; anserinaprion protein HET-s; PFAR

Published in

International Journal of Molecular Sciences
2020, Volume: 21, number: 17, article number: 6340
Publisher: MDPI

SLU Authors

• Pang, Yanhong

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    
  • Uppsala University

UKÄ Subject classification

Biochemistry and Molecular Biology


Publication identifier

DOI: https://doi.org/10.3390/ijms21176340

Permanent link to this page (URI)

https://res.slu.se/id/publ/108111