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Research article2020Peer reviewedOpen access

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

Pang, Yanhong; Kovachev, Petar; Sanyal, Suparna


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.


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

    UKÄ Subject classification

    Biochemistry and Molecular Biology

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