PXD029548

PXD029548 is an original dataset announced via ProteomeXchange.

Title	High-Resolution Complexome-Profiling of Mitochondria Reveals Quality Control Pathways of Protein Import
Description	Mitochondria contain ~1,000 different proteins that may assemble into larger entities such as respiratory (super)complexes and preprotein translocases. The molecular/structural organization of major parts of the mitochondrial proteome, however, has not yet been resolved. We report a quantitative mapping of mitochondrial protein assemblies by high-resolution complexome-profiling of >90% of the yeast mitochondrial proteome, termed MitCOM. Analysis of MitCOM unraveled an unexpected complexity of protein assemblies with each protein found in an average of at least six assemblies. Organization of proteins was distinct between the major classes of mitochondrial function, but independent of their biochemical properties. We detected interactions of the mitochondrial receptor for cytosolic ribosomes, of prohibitin scaffolds and respiratory complexes. Identification of quality control factors operating at the mitochondrial protein entry gate uncovered pathways for preprotein ubiquitylation, deubiquitylation and degradation. MitCOM, made accessible through an interactive viewer on the CEDAR database, may serve as a comprehensive resource for analyzing functional organization and interaction of mitochondrial protein machineries and pathways.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_07:51:37.679.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD029548
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Alexander Haupt
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	2-pyrrolidone-5-carboxylic acid (Glu); 2-pyrrolidone-5-carboxylic acid (Gln); acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2021-11-03 04:35:05	ID requested
1	2023-02-03 23:05:25	announced
⏵ 2	2023-11-14 07:51:40	announced	2023-11-14: Updated project metadata.

Schulte U, den Brave F, Haupt A, Gupta A, Song J, M, ü, ller CS, Engelke J, Mishra S, M, å, rtensson C, Ellenrieder L, Priesnitz C, Straub SP, Doan KN, Kulawiak B, Bildl W, Rampelt H, Wiedemann N, Pfanner N, Fakler B, Becker T, Mitochondrial complexome reveals quality-control pathways of protein import. Nature, 614(7946):153-159(2023) [pubmed]

10.6019/PXD029548;

submitter keyword: complexome, LC-MS, BN-MS, cryo-slicing, mitochondria, BN-PAGE,yeast

Prof. Dr. Bernd Fakler
contact affiliation	Institute of Physiology II Universität Freiburg Germany
contact email	bernd.fakler@physiologie.uni-freiburg.de
lab head
Alexander Haupt
contact affiliation	University of Freiburg, Germany
contact email	alexander.haupt@physiologie.uni-freiburg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/02/PXD029548

PRIDE project URI

• PRIDE
  1. PXD029548
     1. Label: PRIDE project
     2. Name: High-Resolution Complexome-Profiling of Mitochondria Reveals Quality Control Pathways of Protein Import