Stability, Folding, Dimerization, and Assembly Properties of the Yeast Prion Ure2p

The [URE3] factor of Saccharomyces cerevisiae propagates by a prion-like mechanism and corresponds to the loss of the function of the cellular protein Ure2. The molecular basis of the propagation of this phenotype is unknown. We recently expressed Ure2p in Escherichia coli and demonstrated that the...

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Veröffentlicht in:	Biochemistry (Easton) 2001-02, Vol.40 (6), p.1764-1773
Hauptverfasser:	Thual, Carine, Bousset, Luc, Komar, Anton A, Walter, Stefan, Buchner, Johannes, Cullin, Christophe, Melki, Ronald
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyloid - metabolism Circular Dichroism Dimerization Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Fungal Proteins - ultrastructure Glutathione Peroxidase Guanidine Kinetics Molecular Weight Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Peptide Fragments - ultrastructure Prions - chemistry Prions - genetics Prions - metabolism Prions - ultrastructure Protein Denaturation Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - metabolism Recombinant Proteins - ultrastructure Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins Solubility Spectrometry, Fluorescence Ure2 protein
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