Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants

Dergalev, Alexander A.; Alexandrov, Alexander I.; Ivannikov, Roman I.; Ter-Avanesyan, Michael D.; Kushnirov, Vitaly V.

doi:10.3390/ijms20112633

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Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants

Alexander A. Dergalev

Alexander I. Alexandrov

Roman I. Ivannikov

, Michael D. Ter-Avanesyan^† and

Vitaly V. Kushnirov

A.N. Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences, Moscow 119071, Russia

Author to whom correspondence should be addressed.

^†

Michael D. Ter-Avanesyan passed away on 25 October 2018.

Int. J. Mol. Sci. 2019, 20(11), 2633; https://doi.org/10.3390/ijms20112633

Received: 7 May 2019 / Revised: 22 May 2019 / Accepted: 27 May 2019 / Published: 29 May 2019

(This article belongs to the Section Molecular Microbiology)

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Abstract

The yeast [PSI⁺] prion, formed by the Sup35 (eRF3) protein, has multiple structural variants differing in the strength of nonsense suppressor phenotype. Structure of [PSI⁺] and its variation are characterized poorly. Here, we mapped Sup35 amyloid cores of 26 [PSI⁺] ex vivo prions of different origin using proteinase K digestion and mass spectrometric identification of resistant peptides. In all [PSI⁺] variants the Sup35 amino acid residues 2–32 were fully resistant and the region up to residue 72 was partially resistant. Proteinase K-resistant structures were also found within regions 73–124, 125–153, and 154–221, but their presence differed between [PSI⁺] isolates. Two distinct digestion patterns were observed for region 2–72, which always correlated with the “strong” and “weak” [PSI⁺] nonsense suppressor phenotypes. Also, all [PSI⁺] with a weak pattern were eliminated by multicopy HSP104 gene and were not toxic when combined with multicopy SUP35. [PSI⁺] with a strong pattern showed opposite properties, being resistant to multicopy HSP104 and lethal with multicopy SUP35. Thus, Sup35 prion cores can be composed of up to four elements. [PSI⁺] variants can be divided into two classes reliably distinguishable basing on structure of the first element and the described assays. View Full-Text

Keywords: prion; amyloid; prion variants; prion core; proteinase K; Sup35; Rnq1

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MDPI and ACS Style

Dergalev, A.A.; Alexandrov, A.I.; Ivannikov, R.I.; Ter-Avanesyan, M.D.; Kushnirov, V.V. Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants. Int. J. Mol. Sci. 2019, 20, 2633. https://doi.org/10.3390/ijms20112633

AMA Style

Dergalev AA, Alexandrov AI, Ivannikov RI, Ter-Avanesyan MD, Kushnirov VV. Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants. International Journal of Molecular Sciences. 2019; 20(11):2633. https://doi.org/10.3390/ijms20112633

Chicago/Turabian Style

Dergalev, Alexander A., Alexander I. Alexandrov, Roman I. Ivannikov, Michael D. Ter-Avanesyan, and Vitaly V. Kushnirov. 2019. "Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants" International Journal of Molecular Sciences 20, no. 11: 2633. https://doi.org/10.3390/ijms20112633

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Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants

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