Electron Microscopy Study of the Structure of the Sup35 Prion from Yeast Saccharomyces cerevisiae

A. D. Burtseva; Бурцева А. Д.; A. V. Moiseenko; Моисеенко А. В.; T. N. Baymukhametov; Баймухаметов Т. Н.; A. A. Dergalev; Дергалев А. А.; K. M. Boyko; Бойко К. М.; V. V. Kushnirov; Кушниров В. В.

doi:10.31857/S0023476123600817

Electron Microscopy Study of the Structure of the Sup35 Prion from Yeast Saccharomyces cerevisiae

Authors: Burtseva A.D.¹, Moiseenko A.V.², Baymukhametov T.N.³, Dergalev A.A.¹, Boyko K.M.¹, Kushnirov V.V.¹
Affiliations:
1. Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences, 117071, Moscow, Russia
2. Moscow State University, Moscow, Russia
3. National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
Issue: Vol 68, No 6 (2023)
Pages: 874-880
Section: STRUCTURE OF MACROMOLECULAR COMPOUNDS
URL: https://rjeid.com/0023-4761/article/view/673269
DOI: https://doi.org/10.31857/S0023476123600817
EDN: https://elibrary.ru/HAMYDW
ID: 673269

Cite item

Full Text

Open Access
Restricted Access

Access granted
Restricted Access

Subscription or Fee Access

Abstract
About the authors
References
Supplementary files
Statistics

Abstract

Prions form an infectious version of amyloid; they are involved in the pathogenesis of some human neurodegenerative diseases, including Alzheimer’s and Parkinson’s diseases. Yeast prions, in particular, the Sup35 protein, serve an effective model for studying the basic properties of amyloids. Strain versions of the prion form of Sup35 lie in the basis of the conformational diversity of the amyloid structures formed by it, which exhibit different biological properties. The spatial organization of the Sup35 prion has not yet been established. The structure of the strain version W of Sup35 prion protein, isolated ex vivo from yeast Saccharomyces cerevisiae, was studied by transmission electron microscopy (TEM). The parameters of the fibril were estimated, and its structure was reconstructed with a low resolution.

References

Tycko R., Wickner R.B. // Acc. Chem. Res. 2013. V. 46. P. 1487. https://doi.org/10.1021/ar300282r
Sabate R. // Prion. 2014. V. 8. P. 233. https://doi.org/10.4161/19336896.2014.968464
Prusiner S.B. // Science. 1982. V. 216. P. 136. https://doi.org/10.1126/science.6801762
Paushkin S.V. et al. // Science. 1997. V. 277. P. 381. https://doi.org/10.1126/science.277.5324.381
Uptain S.M. // EMBO J. 2001. V. 20. P. 6236. https://doi.org/10.1093/emboj/20.22.6236
Kushnirov V.V. et al. // Prion. 2007. V. 1. P. 179. https://doi.org/10.4161/pri.1.3.4840
Krishnan R., Lindquist S.L. // Nature. 2005. V. 435. P. 765. https://doi.org/10.1038/nature03679
Gorkovskiy A. et al. // Proc. Natl. Acad. Sci. USA. 2014. V. 111. https://doi.org/10.1073/pnas.1417974111
Toyama B.H. et al. // Nature. 2007. V. 449. P. 233. https://doi.org/10.1038/nature06108
Dergalev A. et al. // IJMS. 2019. V. 20. P. 2633. https://doi.org/10.3390/ijms20112633
Ohhashi Y. et al. // Proc. Natl. Acad. Sci. USA. 2018. V. 115. P. 2389. https://doi.org/10.1073/pnas.1715483115
Chernoff Y.O. et al. // Science. 1995. V. 268. P. 880. https://doi.org/10.1126/science.7754373
Scialò C. et al. // Viruses. 2019. V. 11. P. 261. https://doi.org/10.3390/v11030261
Mastronarde D.N. // Microsc Microanal. 2003. V. 9. P. 1182. https://doi.org/10.1017/S1431927603445911
Punjani A. et al. // Nat. Methods. 2017. V. 14. P. 290. https://doi.org/10.1038/nmeth.4169
Makin O.S., Serpell L.C. // FEBS J. 2005. V. 272. P. 5950. https://doi.org/10.1111/j.1742-4658.2005.05025.x
Van Heel M., Schatz M. // J. Struct. Biol. 2005. V. 151. P. 250. https://doi.org/10.1016/j.jsb.2005.05.009
Rosenthal P.B., Henderson R. // J. Mol. Biol. 2003. V. 333. P. 721. https://doi.org/10.1016/j.jmb.2003.07.013
Eanes E.D., Glenner G.G. // J. Histochem. Cytochem. 1968. V. 16. P. 673. https://doi.org/10.1177/16.11.673