The structural basis of yeast prion strain variants

Brandon H. Toyama, Mark J. S. Kelly, John D. Gross and Jonathan S. Weissman ()
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Brandon H. Toyama: Howard Hughes Medical Institute
Mark J. S. Kelly: University of California San Francisco and California Institute for Quantitative Biomedical Research, San Francisco, California 94158-2542, USA
John D. Gross: University of California San Francisco and California Institute for Quantitative Biomedical Research, San Francisco, California 94158-2542, USA
Jonathan S. Weissman: Howard Hughes Medical Institute

Nature, 2007, vol. 449, issue 7159, 233-237

Abstract: A comprehensive structural analysis of the complete and unmodified Sup35 prion domain in two distinct infectious conformations is presented. A variety of techniques is used to provide structural details of these two prion conformations, one weakly and one strongly propagating strain. The data show that the fibril conformation of both strains share a common amyloid-like core, comprising the glutamine/asparagine rich first 40 residues. In the weaker strain this stable structure is dramatically expanded to 70 amino acids.

Date: 2007
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DOI: 10.1038/nature06108

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