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Research article - Peer-reviewed, 2020

Ribosomal RNA Modulates Aggregation of the Podospora Prion Protein HET-s

Pang, Yanhong; Kovachev, Petar; Sanyal, Suparna

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

Authors' information

Swedish University of Agricultural Sciences, Department of Molecular Sciences
Uppsala University
Kovachev, Petar
Uppsala University
Sanyal, Suparna
Uppsala University

UKÄ Subject classification

Biochemistry and Molecular Biology

Publication Identifiers

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

URI (permanent link to this page)

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