Yeast genetics and molecular biology, chaperones and protein misfolding, amyloid and prion diseases, epigenetics and protein-based inheritance. Mylaboratory employsyeast models to studyprionsandamyloids.Prionswere initially identified as proteins in an unusual conformation that cause infectiousneurodegenerativediseases, such as "mad cow" disease,kuruorCreutzfeldt-Jakobdisease. Infection depends on theprion'sability to convert anon-prionprotein, encoded by the same host maintenance gene, into theprionconformation.Prionsform ordered cross-beta fibrous aggregates, termed amyloids. A variety of human diseases, includingAlzheimer'sdisease, are associated with amyloids and possess at least someprionproperties. Someamyloidshave positive biological functions. Manyproteins can formamyloidsin specific conditions. It is thought thatamyloidrepresents one of the ancient types of the protein fold. Some yeastnon-Mendelianheritable elements are based on aprionmechanism. This shows that heritable information can be coded in protein structures, in addition to information coded in DNA sequence. Therefore,prionsprovide a basis for the protein-based inheritance in yeast (and possibly in other organisms). Major topics of research in my lab include cellular control of prion formation and propagation (with a specific emphasis on the role of chaperone proteins), and development of the yeast models forstudying mammalian and humanamyloids, involved in diseases.Our research has demonstrated thatprionscan be induced by transient protein overproduction and discovered the crucial role of chaperones inprionpropagation, shown evolutionary conservation ofprion-formingproperties, established a yeast system for studying species-specificity ofpriontransmission,and uncovered links between prions,cytoskeletalnetworks and protein quality control pathways.