PXD025588

PXD025588 is an original dataset announced via ProteomeXchange.

Title	Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae
Description	Ola1 is implicated in various stress response pathways, as well as in cancer and tumor progression. However, Ola1p functions are divergent between species and still remain poorly understood. Here, we studied the role of Ola1p in the heat shock response in Saccharomyces cerevisiae. We show that deletion of OLA1 results in higher levels of proteins with protective functions for proteome stability under heat stress. We found that Ola1p enriches in detergent-resistant protein aggregates during heat stress. In heat-stressed yeast cells, it rapidly forms assemblies that localize to stress granules. In vitro, Ola1p assembly is protein autonomous and coincides with structural rearrangements that occur at similar temperatures and pH values seen in cells. We further observed that deletion of OLA1 leads to increased ubiquitination of protein aggregates formed during heat stress. Upon stress relief, central factors for protein refolding and the clearance of protein aggregates are synthesized in higher amounts in dola1 cells, whereas global translation reinitiation is decreased in these cells. Our data suggest that Ola1p is a positive factor for stabilizing the misfolded proteome that is sequestered in cytoplasmic stress granules during heat stress and, thereby, enables cells to efficiently restore a functional proteome after stress relief.
HostingRepository	PRIDE
AnnounceDate	2022-02-17
AnnouncementXML	Submission_2022-02-17_00:51:14.601.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Friedel Drepper
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2021-04-23 06:20:21	ID requested
⏵ 1	2022-02-17 00:51:15	announced

Dannenmaier S, Desroches Altamirano C, Sch, ü, ler L, Zhang Y, Hummel J, Milanov M, Oeljeklaus S, Koch HG, Rospert S, Alberti S, Warscheid B, Quantitative proteomics identifies the universally conserved ATPase Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae. J Biol Chem, 297(5):101050(2021) [pubmed]

submitter keyword: native SILAC, Saccharomyces cerevisiae, proteomics, detergent-resistant protein aggregates

Prof. Dr. Bettina Warscheid
contact affiliation	Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and Signalling Research Centres BIOSS and CIBSS, University of Freiburg, 79104 Freiburg im Breisgau, Germany
contact email	Bettina.Warscheid@biologie.uni-freiburg.de
lab head
Friedel Drepper
contact affiliation	AG Warscheid Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany
contact email	friedel.drepper@biologie.uni-freiburg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD025588
     1. Label: PRIDE project
     2. Name: Quantitative proteomics identifies Ola1p as a positive regulator of heat shock response in Saccharomyces cerevisiae