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Peer-reviewedCC BYNature communications

Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotype.

  • Alexander A Dergalev1
  • Yury M Chesnokov2
  • Anna D Burtseva3,4
  • Olga V Mitkevich3
  • Timur N Baymukhametov2
  • Vladimir O Popov3,2
  • Konstantin M Boyko5
  • Vitaly V Kushnirov6
6 affiliations
  1. 1Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia. [email protected].
  2. 2National Research Center "Kurchatov Institute", Moscow, Russia.
  3. 3Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia.
  4. 4Moscow Center for Advanced Studies, Moscow, Russia.
  5. 5Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia. [email protected].
  6. 6Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia. [email protected].
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Abstract

Human prions and amyloids exhibit structural diversity that correlates with different pathological manifestations. Yeast prions represent a convenient model for studying fundamental properties of prions and their strain diversity. The Sup35 yeast prion has multiple structural variants, divided into "strong" and "weak" groups differing in frequency of fibril fragmentation and resulting nonsense-suppression. The molecular origin of these distinctions remains unclear. Here, we show that the different frequency of prion fragmentation is determined by their stability, rather than the efficiency of chaperone binding. The fully protease-resistant part (residues 2-32) of the Sup35 prion core is a key for the prion phenotype and maintenance, whereas partially resistant part (33-72) is less important. We established the cryo-EM structure of a strong Sup35 prion variant purified from yeast, comprising residues 2-64, with 2.7 Å resolution. Comparison of this structure with that of Sup35 amyloid formed in vitro at 4˚C revealed their significant difference.

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Cite

BibTeXRIS
BibTeX
@article{dergalev2026cryoem,
  title = {{Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotype.}},
  author = {Alexander A Dergalev and Yury M Chesnokov and Anna D Burtseva and Olga V Mitkevich and Timur N Baymukhametov and Vladimir O Popov and Konstantin M Boyko and Vitaly V Kushnirov},
  journal = {Nature communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-77823-3},
  url = {https://europepmc.org/article/MED/42901901},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotype.
AU  - Alexander A Dergalev
AU  - Yury M Chesnokov
AU  - Anna D Burtseva
AU  - Olga V Mitkevich
AU  - Timur N Baymukhametov
AU  - Vladimir O Popov
AU  - Konstantin M Boyko
AU  - Vitaly V Kushnirov
PY  - 2026
DA  - 2026/09/19
JO  - Nature communications
DO  - 10.1038/s41467-026-77823-3
UR  - https://europepmc.org/article/MED/42901901
AB  - Human prions and amyloids exhibit structural diversity that correlates with different pathological manifestations. Yeast prions represent a convenient model for studying fundamental properties of prions and their strain diversity. The Sup35 yeast prion has multiple structural variants, divided into "strong" and "weak" groups differing in frequency of fibril fragmentation and resulting nonsense-suppression. The molecular origin of these distinctions remains unclear. Here, we show that the different frequency of prion fragmentation is determined by their stability, rather than the efficiency of chaperone binding. The fully protease-resistant part (residues 2-32) of the Sup35 prion core is a key for the prion phenotype and maintenance, whereas partially resistant part (33-72) is less important. We established the cryo-EM structure of a strong Sup35 prion variant purified from yeast, comprising residues 2-64, with 2.7 Å resolution. Comparison of this structure with that of Sup35 amyloid formed in vitro at 4˚C revealed their significant difference.
SN  - 2041-1723
ER  -