Project title: Role of chaperons in memory formation of yeast
Summary: Prions are amyloid self-propagating heritable protein isoforms. Heritable mode of prions was first proved by using a yeast prion. Lately, a number of prions have been identified in yeast. Prions are known to be associated with diseases in mammals and more importantly have recently been involved in key physiological processes including long-term potentiation and innate immunity. Recently, chaperones including Hsp104, Hsp70 (ssa, ssb) and Hsp40, were shown to play a role in the propagation of prions to daughter cells. Prions are often termed as reproducible memory devices as they generate heritable conformational change in protein. It has been observed that in yeast, pheromone-inducible protein Whi3 forms an uninheritable prion-like super assembly (PrD) in response to opposite partner yeast which saves as memory in mother cells. Primarily, this protein (Whi3) is involved in arresting the cell cycle at G1 upon induction but previous memory of prion like super assembly proteins promote escape from cell cycle arrest leading to budding into daughter cells. Here, we are asking what is the contribution of chaperones to the memory encoded by Whi3 in yeast?