|The School of Molecular and Cellular Biology, University of Illinois, USA
|Molecular chaperones regulate the chromatin landscape: Is it time to move?
|["Molecular chaperones govern protein homeostasis being allied to the beginning (folding) and\r\nending (degradation) of the protein life cycle. Yet, the Hsp90 system primarily associates with\r\nnative factors including fully assembled complexes. The significance of these connections is\r\npoorly understood. To delineate why Hsp90 and its cochaperone p23 interact with mature\r\nfactors we focused on large protein complexes functioning within the nucleus. Evidence will\r\nbe presented demonstrating a role for molecular chaperones both in local chromatin\r\nremodeling events as well as in large-scale chromatin movements. Overall, our results suggest\r\nHsp90 and p23 contribute to proteostasis by chaperoning mature structures through\r\nenergetically unfavorable events thereby maintaining the cellular pool of active native\r\nproteins."]