Protein quality control meets transcriptome remodeling under stress
Authors:Veena Mathew1 and Peter C. Stirling1
1 Terry Fox Laboratory, British Columbia Cancer Agency. 675 West 10th Avenue, Vancouver, British Columbia, V5Z1L3, Canada.
Keywords:
splicing, genotoxic stress, ribosome production, protein aggregate, Saccharomyces cerevisiae.
Corresponding Author(s):
Conflict of interest statement:
The authors declare no conflicts of interest.
Please cite this article as:
Veena Mathew, Peter C. Stirling (2017). Protein quality control meets transcriptome remodeling under stress. Cell Stress 1(3): 134-135. doi: 10.15698/cst2017.12.115
© 2017 Mathew and Stirling. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
Abstract:
To tolerate and recover from genotoxic stress cells must coordinate a range of stress response activities including cell cycle arrest, DNA repair, and remodeling of the transcriptome and proteome. The suppression of ribosome production is a key feature of many stress responses in yeast, and much is known about the dynamics of this process at the transcriptional level. In our recent study, (J Cell Biol doi: 10.1083/ jcb.201612018) we focus on the stress related dynamic behaviour of a splicing factor called Hsh155, which is a core component of the SF3B subcomplex of the U2 small nuclear ribonucleoprotein complex, homologous to human SF3B1. The disassembly from its complex and sequestration of Hsh155 into nuclear protein aggregates contributes to suppressing ribosome production post-transcriptionally by promoting intron retention in ribosomal protein gene transcripts. The relocalization of Hsh155 is facilitated by TORC1-driven transcriptional changes and molecular chaperones that recognize disassembled Hsh155, eventually aiding in efficient recovery from stress.