The Hsp90 Molecular Chaperone Regulates the Transcription Factor Network Controlling Chromatin Accessibility.

ABSTRACT: Genomic events including gene regulation and chromatin status are controlled by transcription factors. Here we report that the Hsp90 molecular chaperone broadly regulates the transcription factor protein family. Our studies identified a biphasic use of Hsp90 in which early inactivation (15 min) of the chaperone triggered a wide reduction of DNA binding events along the genome with concurrent changes to chromatin structure. Long-term loss (6 h) of Hsp90 resulted in a decline of a divergent yet overlaying pool of transcription factors that produced a distinct chromatin pattern. Although both phases involve protein folding, the early point correlated with Hsp90 acting in a late folding step that is critical for DNA binding function, whereas prolonged Hsp90 inactivation led to a significant de

SUBMITTER: Gvozdenov Z 

PROVIDER: S-EPMC6983977 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature