Correlation Engine 2.0
Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

Global repression of protein synthesis is a hallmark of the cellular stress response and has been attributed primarily to inhibition of translation initiation, although this mechanism may not always explain the full extent of repression. Here, using ribosome footprinting, we show that 2 hr of severe heat stress triggers global pausing of translation elongation at around codon 65 on most mRNAs in both mouse and human cells. The genome-wide nature of the phenomenon, its location, and features of protein N termini suggested the involvement of ribosome-associated chaperones. After severe heat shock, Hsp70's interactions with the translational machinery were markedly altered and its association with ribosomes was reduced. Pretreatment with mild heat stress or overexpression of Hsp70 protected cells from heat shock-induced elongation pausing, while inhibition of Hsp70 activity triggered elongation pausing without heat stress. Our findings suggest that regulation of translation elongation in general, and by chaperones in particular, represents a major component of cellular stress responses. Copyright © 2013 Elsevier Inc. All rights reserved.

Citation

Reut Shalgi, Jessica A Hurt, Irina Krykbaeva, Mikko Taipale, Susan Lindquist, Christopher B Burge. Widespread regulation of translation by elongation pausing in heat shock. Molecular cell. 2013 Feb 07;49(3):439-52

Expand section icon Mesh Tags

Expand section icon Substances


PMID: 23290915

View Full Text