PXD017847

PXD017847 is an original dataset announced via ProteomeXchange.

Title	Specific features and assembly of the plant mitochondrial complex I revealed by cryo-EM
Description	Mitochondria are the powerhouses of eukaryotic cells and the site of essential metabolic reactions. Their main purpose is to maintain the high ATP/ADP ratio that is required to fuel the countless biochemical reactions taking place in eukaryotic cells1. This high ATP/ADP ratio is maintained through oxidative phosphorylation (OXPHOS). Complex I or NADH:ubiquinone oxidoreductase is the main entry site for electrons into the mitochondrial respiratory chain and constitutes the largest of the respiratory complexes2. Its structure and composition varies across eukaryotes species. However, high resolution structures are available only for one group of eukaryotes, opisthokonts3–6. In plants, only biochemical studies were carried out, already hinting the peculiar composition of complex I in the green lineage. Here, we report several cryo-electron microscopy structures of the plant mitochondrial complex I at near-atomic resolution. We describe the structure and composition of the plant complex I including the plant-specific additional domain composed by carbonic anhydrase proteins. We show that the carbonic anhydrase is an heterotrimeric complex with only one conserved active site. This domain is crucial for the overall stability of complex I as well as a peculiar lipid complex composed cardiolipin and phosphatidylinositols. Moreover we also describe the structure of one of the plant-specific complex I assembly intermediate, lacking the whole PD module, in presence of the maturation factor GLDH. GLDH prevents the binding of the plant specific P1 protein, responsible for the linkage of the PP to the PD module. Finally, as the carbonic anhydrase domain is likely to be associated with complex I from numerous other known eukaryotes, we propose that our structure unveils an ancestral-like organization of mitochondrial complex I.
HostingRepository	PRIDE
AnnounceDate	2020-10-26
AnnouncementXML	Submission_2020-10-26_00:49:33.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD017847
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Lauriane Kuhn
SpeciesList	scientific name: Brassica oleracea var. botrytis (Cauliflower); NCBI TaxID: 3715;
ModificationList	Phospho; Oxidation; Acetyl; Carbamidomethyl
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2020-03-03 09:12:50	ID requested
⏵ 1	2020-10-26 00:49:34	announced

Soufari H, Parrot C, Kuhn L, Waltz F, Hashem Y, Specific features and assembly of the plant mitochondrial complex I revealed by cryo-EM. Nat Commun, 11(1):5195(2020) [pubmed]

submitter keyword: complex I, mitochondria, plant, cryo-EM, shotgun proteomics

Florent Waltz
contact affiliation	Institut Européen de Chimie et Biologie, U1212 Inserm, Université de Bordeaux, 2 rue R. Escarpit, F-33600 Pessac, France.
contact email	waltz.florent@gmail.com
lab head
Lauriane Kuhn
contact affiliation	CNRS, IBMC, FRC1589
contact email	l.kuhn@ibmc-cnrs.unistra.fr
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/2020/10/PXD017847

PRIDE project URI

• PRIDE
  1. PXD017847
     1. Label: PRIDE project
     2. Name: Specific features and assembly of the plant mitochondrial complex I revealed by cryo-EM