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Vol 51(2017) N 2 p. 323-327; DOI 10.1134/S0026893317010058 Full Text

S.A. Bondarev1,2*, D.V. Likholetova1, M.V. Belousov1, G.A. Zhouravleva1,2

Rnq1 protein protects [PSI+] prion from effect of the PNM mutation

1Laboratory of Physiological Genetics, Department of Genetics and Biotechnology, St. Petersburg State University, St. Petersburg, 199034 Russia
2Laboratory of Amyloid BiologySt. Petersburg State University, St. Petersburg, 199034 Russia


*stanislavspbgu@gmail.com
Received - 2016-03-09; Accepted - 2016-04-11

The interaction of [PSI+] and [PIN+] factors in yeast Saccharomyces cerevisiae is known as the first evidence of prions networks. In [PIN+] cells, Rnq1p prion aggregates work as a template for Sup35p aggregation, which is essential for [PSI+] induction. No additional factors are required for subsequent Sup35p aggregation. Nevertheless, several recent reports provide data that indicate a more complex interplay between these prions. Our results show that the presence of Rnq1p in the cell significantly decreases the loss of [PSI+] prion, which is caused by a double mutation in SUP35 (Q61K, Q62K substitutions in the Sup35 protein). These observations support the existence of interaction networks that converge on a strong linkage of prionogenic and prion-like proteins, and the participation of Rnq1 protein in the maintenance of prion [PSI+].

Prions, amyloids, SUP35, RNQ1, [PSI+], [PIN+], mutations, yeasts



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