PXD059828-1

PXD059828 is an original dataset announced via ProteomeXchange.

Title	Prevention of mitochondrial proteotoxicity by formation of a chaperone-dependent protective shell around aggregated polypeptides
Description	The potential proteotoxicity of mitochondrial aggregates in yeast cells is reduced by a sequestration of affected polypeptides into a mitochondrial protein quality control compartment (IMiQ). Based on the expression of an aggregation-prone protein in the mitochondrial matrix, we determined the effect of organelle dynamics on aggregate sequestration. Fusion deficient cells were unable to accumulate the aggregates in the IMiQ, resulting in a stress-sensitive phenotype. In contrast, fission deficient cells could not separate the aggregate from the mitochondrial network. In these mitochondria, the aggregates were neutralized by the formation of a shell formed by mitochondrial chaperones. We also performed quantitative mass spectrometry to analyse the mitochondrial proteome and the extent of co-aggregation of mitochondrial proteins. While only minor changes of the total proteome were detected in response to aggregate accumulation, we found a recruitment of proteins of the respiration complexes and of the protein quality control system (PQC). In particular members of the Hsp70 chaperone family were prominently associated with the aggregate. We conclude that this chaperone-dependent neutralization prevents a major co-aggregation of endogenous mitochondrial proteins.
HostingRepository	PRIDE
AnnounceDate	2025-08-21
AnnouncementXML	Submission_2025-08-21_04:52:38.226.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD059828
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
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2025-01-15 09:56:22	ID requested
⏵ 1	2025-08-21 04:52:40	announced

10.1242/jcs.263680;

10.6019/PXD059828;

Ruland L, Sylvester M, Maus L, Beckert H, Voos W, Mitochondrial protein aggregates recruit key chaperones and are sequestered in a fission- and fusion-dependent process. J Cell Sci, 138(16):(2025) [pubmed]

submitter keyword: mitochondria, Hsp70, chaperone, protein aggregation, proteostasis,yeast

Prof. Dr. Wolfgang Voos
contact affiliation	Institute of Biochemistry and Molecular Biology, Faculty of Medicine, University of Bonn, 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. PXD059828
     1. Label: PRIDE project
     2. Name: Prevention of mitochondrial proteotoxicity by formation of a chaperone-dependent protective shell around aggregated polypeptides