Sammanfattning

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.

Nyckelord

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

Publicerad i

International Journal of Molecular Sciences
2020, Volym: 21, nummer: 17, artikelnummer: 6340
Utgivare: MDPI

SLU författare

• Pang, Yanhong

  • Institutionen för molekylära vetenskaper, Sveriges lantbruksuniversitet
    
  • Uppsala universitet

UKÄ forskningsämne

Biokemi och molekylärbiologi


Publikationens identifierare

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

Permanent länk till denna sida (URI)

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