PXD030436-1

PXD030436 is an original dataset announced via ProteomeXchange.

Title	Proteomic characterization of Hsp78-interacting proteins highlights chaperone role during protein aggregation in mitochondria under heat stress - Part B Aggregation
Description	Chaperones of the Hsp100 chaperone family support protein homeostasis, the maintenance of protein activity under stress, by refolding aggregated proteins or targeting them for degradation. Hsp78, the ClpB-type mitochondrial member of the Hsp100 family, can be found in lower eukaryotes like yeast. Although Hsp78 has been shown to contribute to protection against elevated temperatures in yeast, the biochemical mechanisms underlying this mitochondria-specific thermotolerance are still largely unclear. To identify endogenous chaperone substrate proteins, we generated an Hsp78-ATPase mutant with a stabilized substrate binding behavior. We used two SILAC-based quantitative mass spectrometry approaches to analyze the role of Hsp78 during heat stress-induced mitochondrial protein aggregation and disaggregation processes on a proteomic level. In the first setup, Hsp78-interacting polypeptides were identified to reveal the endogenous substrate spectrum of the chaperone. Our analysis revealed that Hsp78 is interacting with a wide variety of proteins related to metabolic functions including energy production and protein synthesis, as well as other chaperones, thus maintaining crucial functions for mitochondrial stress resistance. We compared these interaction data with a second experimental setup that focused on the on overall aggregation and disaggregation processes in mitochondria under heat stress on a proteomic level. This revealed specific aggregation-prone protein populations and demonstrated the direct quantitative impact of Hsp78 on stress-dependent protein solubility different conditions and. We conclude that Hsp78 together with its cofactors represents a recovery system that protects major mitochondrial metabolic functions during as well restores protein biogenesis capacity after heat stress.
HostingRepository	PRIDE
AnnounceDate	2024-10-07
AnnouncementXML	Submission_2024-10-07_13:44:34.370.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD030436
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Marc Sylvester
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	S-carboxamidoethyl-L-cysteine; 6x(13)C; (4,4,5,5-(2)H4)-L-lysine; isotope labeled residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2021-12-16 01:57:38	ID requested
⏵ 1	2024-10-07 13:44:34	announced

10.1016/J.JBC.2022.102494;

10.6019/PXD030436;

submitter keyword: Hsp78,Yeast, cell biology, mitochondria, chaperone, protein aggregation, proteostasis, heat stress

Wolfgang Voos
contact affiliation	nstitute of Biochemistry and Molecular Biology (IBMB), Faculty of Medicine, University of Bonn, Nussallee 11, 53115 Bonn, Germany
contact email	wolfgang.voos@uni-bonn.de
lab head
Marc Sylvester
contact affiliation	Institute of Biochemistry and Molecular Biology, Medical Faculty, University of Bonn
contact email	msylvest@uni-bonn.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD030436
     1. Label: PRIDE project
     2. Name: Proteomic characterization of Hsp78-interacting proteins highlights chaperone role during protein aggregation in mitochondria under heat stress - Part B Aggregation