The Role of the R2TP Chaperone Complex in Liquid Phase Separation

Abstract: Ensuring the proper folding and assembly of proteins is essential for maintaining the proper functioning of cells. This important task is accomplished by a complex network of proteins known as molecular chaperones including the highly conserved Hsp90 chaperone complex. Our group recently discovered the R2TP chaperone complex consisting of RUVBL1-RUVBL2-RPAP3-PIH1D1, which interacts with Hsp90 to mediate the assembly of various large complexes important for regulating cell growth and proliferation. Currently, a detailed mechanism how R2TP assembles these large complexes is unknown. Thus, my research will focus on characterizing and understanding the function of this chaperone through its role in regulating RNA polymerase II CTD condensate formation. Recent evidence has shown that molecular chaperones and ATP modulate biomolecular condensate formation in cells. We found that the droplet size and condensate fractions of CTD increases in the presence of RUVBL1/2 in an ATP dependent manner. Additional assays have indicated that RUVBL1/2 act as ATP-driven remodelers that promote CTD condensate formation. This talk will discuss the role of RUVBL1/2 ATPase activity in controlling RNA polymerase II CTD condensate formation and discuss implications for transcription regulation.

Bio: Maryama Mohamed is PhD student in the Houry group. Her work currently focuses functionally characterizing the role the R2TP chaperone complex.

Zoom Link available on request by emailing haissi.cui@utoronto.ca

CHM 1090 Students, please see Quercus for full speaker schedule.