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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
Published on: July 9, 2013
Dynamic global acetylation remodeling during the yeast heat shock response
Rebecca E Hardman-Kavanaugh1,2, Aaron J Storey3, Tara N Stuecker2
1Interdisciplinary Graduate Program in Cell and Molecular Biology, University of Arkansas, Fayetteville, AR, 72701, USA.
Genome Biology
|July 17, 2026
Summary
Global protein acetylation plays a key role in the heat shock response. This study reveals how changes in acetylation regulate protein activity, aiding cellular survival under stress conditions.
Area of Science:
- Molecular Biology
- Cellular Stress Response
- Proteomics
Background:
- Organisms require rapid responses to environmental stress.
- Post-translational protein modifications, like lysine acetylation, rapidly modulate protein activity.
- The function of acetylation for most proteins remains largely unknown.
Purpose of the Study:
- To investigate the role of global acetylation in the heat shock response of Saccharomyces cerevisiae.
- To understand how protein acetylation impacts cellular heat sensitivity.
Main Methods:
- Proteomic analysis of the yeast acetylome under heat shock conditions.
- Quantification of changes in protein acetylation marks.
- Correlation of acetylation changes with gene expression data.
Main Results:
- Global acetylation is crucial for the heat shock response; dysregulation causes heat sensitivity.
- The yeast acetylome is globally remodeled during heat shock, with significant changes in ~200 proteins.
- Proteins with altered acetylation overlap with heat shock-induced/repressed genes, including chaperones and ribosomal proteins.
Conclusions:
- Protein acetylation activates induced proteins and inactivates repressed proteins during heat shock.
- Acetylation may function similarly to histone marks in regulating protein activity.
- This study reveals a new layer of post-translational regulation augmenting the heat shock response.
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