Berthelot K, Immel F, Géan J, Lecomte S, Oda R, Kauffmann B, Cullin C.
Driving amyloid toxicity in a yeast model by structural changes: a molecular approach.
FASEB J. 2009 Jul;23(7):2254-63.
PubMed.
Berthelot and colleagues describe the structure and toxicity of a mutant form of the normally benign, model amyloid protein (Het-s218-289) in yeast. The model, though involving an artificial protein construct, yields a clear correlation between structural changes (assessed with multiple methodologies) and cytotoxicity. The findings suggest that the mutant protein forms a stable assembly that mimics the toxic intermediates that may contribute to the pathogenicity of proteins in various diseases. The molecular variations that influence toxicity in vertebrate proteopathies are more subtle than those in the model protein of Berthelot et al., but this interesting yeast paradigm enables an efficient and comprehensive analysis of the process in vivo that might ultimately have applicability to Alzheimer disease and other disorders involving protein aggregation.
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Emory University
Berthelot and colleagues describe the structure and toxicity of a mutant form of the normally benign, model amyloid protein (Het-s218-289) in yeast. The model, though involving an artificial protein construct, yields a clear correlation between structural changes (assessed with multiple methodologies) and cytotoxicity. The findings suggest that the mutant protein forms a stable assembly that mimics the toxic intermediates that may contribute to the pathogenicity of proteins in various diseases. The molecular variations that influence toxicity in vertebrate proteopathies are more subtle than those in the model protein of Berthelot et al., but this interesting yeast paradigm enables an efficient and comprehensive analysis of the process in vivo that might ultimately have applicability to Alzheimer disease and other disorders involving protein aggregation.
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