Datasets

Title	Persistent activation of mRNA translation by transient Hsp90 inhibition
Organism
Number of Samples	6
Release Date	2020/07/07 00:00
Sequencing Types
Protocol Details

Title
Authors	Tsvetkov P,Eisen TJ,Heinrich SU,Brune Z,Hallacli E,Newby GA,Kayatekin C,Pincus D,Lindquist S
Journal	Cell reports
Publication Date	2020 Aug 11
Abstract	The heat shock protein 90 (Hsp90) chaperone functions as a protein-folding buffer and plays a role promoting the evolution of new heritable traits. To better understand how Hsp90 can affect mRNA translation, we screen more than 1,600 factors involved in mRNA regulation for physical interactions with Hsp90 in human cells. The mRNA binding protein CPEB2 strongly binds Hsp90 via its prion domain. In a yeast model, transient inhibition of Hsp90 results in persistent activation of a CPEB translation reporter even in the absence of exogenous CPEB that persists for 30 generations after the inhibitor is removed. Ribosomal profiling reveals that some endogenous yeast mRNAs, including HAC1, show a persistent change in translation efficiency following transient Hsp90 inhibition. Thus, transient loss of Hsp90 function can promote a nongenetic inheritance of a translational state affecting specific mRNAs, introducing a mechanism by which Hsp90 can promote phenotypic variation. Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.
PMC	PMC10088179
PMID	32783929
DOI

Tsvetkov et al. 2020 (PRJNA644594)