Jill Johnson Publishes Paper on Heat Shock Proteins in Nature CommunicationsApril 17, 2019
Professor Jill Johnson, in collaboration with researchers at the University of Alberta and the University of Würzburg, recently published a paper in Nature Communications titled: “The conserved NxNNWHW Motif in Aha1-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation and is essential for in vivo function.” This research seeks to understand how Hsp90 partners with interacting cochaperones to help 10-15% of cellular proteins fold properly. As part of an IBEST pilot grant award to Dr. Johnson, she identified a version of Hsp90 that increases the requirement for specific cochaperones, allowing more detailed analysis of their function. Hsp90 binds and hydrolyzes ATP, but the link between this activity and function remains unclear. This work suggests that one type of cochaperone regulates a critical step that occurs after ATP hydrolysis. Future collaborative efforts will lead to a greater understanding of Hsp90 function, with the eventual goal of learning how changes in nucleotide release affect the ability of Hsp90 to interact with misfolded proteins.