Structural biology of prion formation and transmission in yeast

Toshinobu Shida, Motomasa Tanaka

Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
Laboratory for Protein Confirmation Diseases, RIKEN Brain Science Institute

　　Prion diseases are caused by aggregation of the human prion protein in brain and belong to a class of fatal progressive neurodegenerative disorders in mammals.　Yet, the mechanism of how a prion protein becomes a toxic, infectious agent in vivo remains largely unknown.　Prion-like proteins have also been discovered in yeast, collectively known as “yeast prions”, and have been studied extensively to elucidate the molecular mechanisms of conformational variation, transmission, and their biological roles. In this review, we highlight recent advances in our understanding of the structural aspects of the yeast prion protein Sup35.

Address correspondence to Dr. Motomasa Tanaka, Laboratory for Protein Confirmation Diseases, RIKEN Brain Science Institute(2-1 Wako City, Saitama, 351-0198, Japan)