Prions are self-templating alternative folds of proteins. The best-known example of this remarkable group of proteins is PrP – transmission agent responsible for causing “Mad Cow Disease.” Besides PrP, other prion proteins exist and are now attracting attention because of their benign functions in microbes. Our research focuses on conserved prion-like proteins that can be found across the tree of life. During the lecture, I will discuss our discovery of prion-like heritable aggregates in Archaea and provide an evolutionary perspective on prion-like aggregation. I will discuss the potentially widespread role of protein-based inheritance in adapting microorganisms to changing environmental conditions. I will also talk about other similar to prions, forms of self-templating protein aggregates – amyloids – their role in biofilm formation, and the possible role as the first catalyst in the origin of life.<\/p>\n\n