COMPARISON OF CRUDE LYSATE PELLETS OF ISOGENIC STRAINS OF YEAST WITH DIFFERENT PRION COMPOSITION: IDENTIFICATION OF A SET OF
PRION-ASSOCIATED PROTEINS
O. V. Nevzglyadova,1 A. V. Artemov,1 A. G. Mittenberg,1 E. I. Kostyleva,1
E. V. Mikhailova,1 K. V. Solovyov,2 I. M. Kuznetsova,1 K. K. Turoverov,1 T. R. Soidla 1
1 Institute of Cytology RAS, and 2 Institute of Experimental Medicine RAMS, St. Petersburg;
e-mail: oneva43@yahoo.com
A new approach: comparative analysis of proteins of the pellets of crude cell lysates of isogenic strains of Saccharomyces cerevisiae differing by their prion
composition permitted to identify a large group of prion-asso-ciated proteins in yeast cells. 2D-electrophoresis followed by MALDI-analysis of a recipient
[psi-] strain and of [ŠSI+] cytoductant led to identification of 35 proteins whose aggregation state responded to a shift of prion(s)
content. Approximately half of these proteins belonged to functional groups of chaperones and enzyme involved in glucose metabolism. Notable were also proteins involved
in translation, in oxidative stress response and in protein degradation. The data obtained are compared with the results of other groups who used other approaches to
detecting proteins involved in prion aggregates.
Key words: amyloid, prion, heterokaryon, cytoduction, Saccharomyces cerevisiae
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