Research Projects

The Saccharomyces cerevisiae Stm1 protein is a crucial ribosomal association factor that plays a crucial role in various biological functions. It preserves ribosome under nutrition-deprived conditions by repressing ribosomal translation through binding into the mRNA binding tunnel. Recent studies have shown that the purine motif DNA triplex and G-quadruplex recognizing Stm1 N-terminal region self-perpetuates to form concentration-dependent amyloid conformation, explaining Stm1 overexpression in apoptosis-like cell death. However, the role of Stm1 C-terminus (Stm1_C) and interaction of nucleic acids triplex/quadruplex with Stm1_N in regulating the amyloid formation of Stm1 full-length (Stm1_FL) is unknown. The authors hypothesize that Stm1_C, an unstructured protein with a liquid-liquid phase separation prone RGG motif, may enhance the amyloidogenic character of Stm1_FL at higher concentrations and facilitate apoptosis-like cell death in Saccharomyces cerevisiae. Additionally, nucleic acid triplex/quadruplex may play an antagonist's role for the amyloid conformational preference of Stm1_FL, deciding to retain the monomeric conformation of Stm1_FL to facilitate interaction with ribosome. The researchers propose exploring the amyloidogenic nature of Stm1_C and Stm1_FL, as well as the role of nucleic acids triplex/quadruplex in regulating the amyloidogenic character of Stm1_FL using CD, Th-T kinetics, and AFM.