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A size threshold limits prion transmission and establishes phenotypic diversity.
- Source :
-
Science (New York, N.Y.) [Science] 2010 Oct 29; Vol. 330 (6004), pp. 680-3. - Publication Year :
- 2010
-
Abstract
- According to the prion hypothesis, atypical phenotypes arise when a prion protein adopts an alternative conformation and persist when that form assembles into self-replicating aggregates. Amyloid formation in vitro provides a model for this protein-misfolding pathway, but the mechanism by which this process interacts with the cellular environment to produce transmissible phenotypes is poorly understood. Using the yeast prion Sup35/[PSI(+)], we found that protein conformation determined the size distribution of aggregates through its interactions with a molecular chaperone. Shifts in this range created variations in aggregate abundance among cells because of a size threshold for transmission, and this heterogeneity, along with aggregate growth and fragmentation, induced age-dependent fluctuations in phenotype. Thus, prion conformations may specify phenotypes as population averages in a dynamic system.
- Subjects :
- Algorithms
Cell Division
Computer Simulation
Peptide Termination Factors metabolism
Phenotype
Prions metabolism
Protein Conformation
Protein Folding
Recombinant Fusion Proteins chemistry
Saccharomyces cerevisiae cytology
Saccharomyces cerevisiae Proteins metabolism
Peptide Termination Factors chemistry
Prions chemistry
Saccharomyces cerevisiae chemistry
Saccharomyces cerevisiae Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 330
- Issue :
- 6004
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 21030659
- Full Text :
- https://doi.org/10.1126/science.1197785