PXD063569-1

PXD063569 is an original dataset announced via ProteomeXchange.

Title	Dynamic global acetylation remodeling during the yeast heat shock response
Description	All organisms experience stress and must rapidly respond to changing conditions. Thus, cells have evolved sophisticated rapid-response mechanisms such as post-translational protein modification to rapidly and reversibly modulate protein activity. One such post-translational modification is reversible lysine acetylation, where proteomic studies have identified thousands of acetylated proteins across diverse organisms. While the sheer size of the 'acetylome' is striking, the function of acetylation for the vast majority of proteins remains largely obscure. Here, we show that global acetylation plays a previously unappreciated role in the heat shock response of Saccharomyces cerevisiae. We find that dysregulated acetylation renders cells heat sensitive, and moreover, that the acetylome is globally remodeled during heat shock over time. Using quantitative acetyl-proteomics, we identified ~400 high-confidence acetyl marks across ~200 proteins that significantly change in acetylation when cells are shifted to elevated temperature. Proteins with significant changes in lysine acetylation during heat shock strongly overlap with genes induced or repressed by stress. Thus, we hypothesize that protein acetylation augments the heat shock response by activating induced proteins and inactivating repressed proteins. Intriguingly, we find nearly 40 proteins with at least two acetyl marks that significantly change in the opposite directions. These proteins are strongly enriched for chaperones and ribosomal proteins, suggesting that these two key processes are coordinately regulated by protein acetylation during heat shock. Moreover, we hypothesize that the same type of activating and inactivating marks that exist on histones may be a general feature of proteins regulated by acetylation. Overall, this work has identified a new layer of post-translational regulation that likely augments the classic heat shock response.
HostingRepository	PRIDE
AnnounceDate	2025-05-03
AnnouncementXML	Submission_2025-05-03_05:18:40.813.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD063569
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Jeffrey Lewis
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2025-05-02 12:43:43	ID requested
⏵ 1	2025-05-03 05:18:41	announced

10.6019/PXD063569;

10.1101/2025.01.10.632339;

Hardman-Kavanaugh RE, Storey AJ, Stuecker TN, Hood SE, Barrett-Wilt GA, Krishnamurthi VR, Wang Y, Byrum SD, Mackintosh SG, Edmondson RD, Wahls WP, Tackett AJ, Lewis JA, Dynamic global acetylation remodeling during the yeast heat shock response. bioRxiv, ():(2025) [pubmed]

submitter keyword: acetylome, heat shock, TMT, stress,yeast

Jeffrey A. Lewis
contact affiliation	Department of Biological Sciences, University of Arkansas, USA
contact email	lewisja@uark.edu
lab head
Jeffrey Lewis
contact affiliation	University of Arkansas
contact email	lewisja@uark.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD063569
     1. Label: PRIDE project
     2. Name: Dynamic global acetylation remodeling during the yeast heat shock response