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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, Arkansas 72701, United States of America.
Biorxiv : the Preprint Server for Biology
|February 12, 2025
Summary
Global protein acetylation plays a key role in the heat shock response. This study reveals how lysine acetylation regulates protein activity during heat stress in yeast, uncovering a new layer of cellular regulation.
Area of Science:
- Molecular Biology
- Cellular Stress Response
- Proteomics
Background:
- Organisms require rapid responses to environmental stress.
- Post-translational modifications, like lysine acetylation, are crucial for modulating 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 identify proteins and acetylation sites dynamically regulated during heat shock.
- To elucidate how protein acetylation contributes to cellular adaptation to heat stress.
Main Methods:
- Quantitative acetyl-proteomics to profile changes in the acetylome.
- Analysis of protein acetylation patterns under heat shock conditions.
- Bioinformatic analysis to identify overlapping proteins with stress-responsive genes.
Main Results:
- Dysregulated acetylation leads to heat sensitivity in yeast cells.
- The yeast acetylome is globally remodeled during heat shock.
- ~400 acetylation sites on ~200 proteins significantly change during heat stress, overlapping with stress-induced genes.
- Coordinated regulation of chaperones and ribosomal proteins by acetylation during heat shock was observed.
Conclusions:
- Protein acetylation augments the heat shock response by activating or inactivating proteins.
- Lysine acetylation represents a significant regulatory mechanism in cellular stress adaptation.
- This study identifies a novel layer of post-translational regulation in the heat shock response.
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