[PIN+]-dependent induction of protease-resistant amyloids by Ade2p protein fused with prionizing NM domain of Sup35 protein of the yeast Saccharomyces cerevisiae

This work studied the dependence of the formation of insoluble aggregates containing Sup35 and NM Ade2 proteins on the presence of [PSI+] prion in the cells. .

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Bibliographic Details
Published in:Doklady. Biochemistry and biophysics 2010-08, Vol.433 (1), p.183-186
Main Authors: Pogoda, A. A., Alenin, V. V., Borchsenius, A. S., Zadorsky, S. P., Manukhov, V. V., Inge-Vechtomov, S. G.
Format: Article
Language:English
Subjects:
Amyloidogenic Proteins - chemistry
Amyloidogenic Proteins - metabolism
Binding Sites
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Biophysics and Molecular Biology
Life Sciences
Peptide Hydrolases - chemistry
Peptide Hydrolases - metabolism
Peptide Termination Factors - chemistry
Peptide Termination Factors - metabolism
Prions
Proteases
Protein Binding
Protein Structure, Tertiary
Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Yeast
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Description
Summary:This work studied the dependence of the formation of insoluble aggregates containing Sup35 and NM Ade2 proteins on the presence of [PSI+] prion in the cells. .
ISSN:1607-6729
1608-3091
DOI:10.1134/S1607672910040101