Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates.

doi:10.1006/jmbi.2001.5234

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Article

Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates.

Journal of molecular biology - 11 Jan 2002

Galani Despina, Fersht Alan R, Perrett Sarah

Abstract excerpt

The Saccharomyces cerevisiae non-Mendelian factor [URE3] propagates by a prion-like mechanism, involving aggregation of the chromosomally encoded protein Ure2. The N-terminal prion domain (PrD) of Ure2 is required for prion activity in vivo and amyloid formation in vitro. However, the molecular mechanism of the prion-like activity remains obscure. Here we measure the kinetics of folding of Ure2 and two N-terminal...

Topics

Amyloidosis
Dimerization
Fluorescence
Glutathione Peroxidase
Guanidine
Isomerism
Kinetics
Models, Biological
Mutation
Prions
Proline
Protein Denaturation
Protein Folding
Protein Renaturation
Protein Structure, Tertiary
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Solutions

Source

Open in PubMed

Identifiers

PMID: 11779240
DOI: 10.1006/jmbi.2001.5234

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