PXD044071

PXD044071 is an original dataset announced via ProteomeXchange.

Title	The divergent ER-mitochondria encounter structures (ERMES) are conserved in parabasalids but lost in several anaerobic lineages with hydrogenosomes.
Description	The endoplasmic reticulum (ER)-mitochondria membrane contact sites (MCS) are extensively studied in aerobic eukaryotes, however, little is known about MCS in anaerobes with reduced forms of mitochondria named hydrogenosomes. In several eukaryotic lineages, the direct physical tether between ER and the outer mitochondrial membrane is formed by ER-mitochondria encounter structure (ERMES). The complex consists of four core proteins (Mmm1, Mmm2, Mdm12, and Mdm10) which are involved in phospholipid trafficking. Here we investigated ERMES distribution in organisms bearing hydrogenosomes and employed Trichomonas vaginalis as a model to estimate ERMES cellular localization, structure, and function. Homology searches revealed that Parabasalia-Anaeramoebae, anaerobic jakobids, and anaerobic fungi are lineages with hydrogenosomes that retain ERMES, while ERMES components were gradually lost in Fornicata, and are absent in Preaxostyla, and Archamoebae. In T. vaginalis and other parabasalids, three ERMES components were found with the expansion of Mmm1. Immunofluorescence microscopy confirmed that Mmm1 localized in ER, while Mdm12 and Mmm2 were partially localized in hydrogenosomes. Pull-down assays and mass spectrometry of the ERMES components identified a parabasalid-specific Porin2 as a substitute for the Mdm10. ERMES modeling showed a formation of a continuous hydrophobic tunnel of TvMmm1-TvMdm12-TvMmm2 that is anchored via Porin2 to the hydrogenosomal outer membrane. Phospholipid-ERMES docking and Mdm12-phospholipid dot-blot indicated that ERMES is involved in the transport of phosphatidylinositol phosphates. However, the absence of enzymes involved in mitochondrial phospholipid metabolism, Psd1, and cardiolipin synthase, indicates that ERMES is not involved in the exchange of substrates for lipid metabolism between ER and hydrogenosomes.
HostingRepository	PRIDE
AnnounceDate	2023-10-03
AnnouncementXML	Submission_2023-10-03_07:36:52.222.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	KarelHarant
SpeciesList	scientific name: Trichomonas vaginalis; NCBI TaxID: 5722;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2023-07-25 07:54:13	ID requested
⏵ 1	2023-10-03 07:36:52	announced

Dataset with its publication pending

submitter keyword: hydrogenosomes, Trichomonas vaginalis, anaerobiosis, endoplasmatic reticulum,ERMES

prof. RNDr. Jan Tachezy,Ph.D.
contact affiliation	Charles University in Prague, Faculty of Science Department of Parasitology Biocev, Průmyslová 595, Vestec 252 42
contact email	jan.tachezy@natur.cuni.cz
lab head
KarelHarant
contact affiliation	Charles University
contact email	harant@natur.cuni.cz
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD044071
     1. Label: PRIDE project
     2. Name: The divergent ER-mitochondria encounter structures (ERMES) are conserved in parabasalids but lost in several anaerobic lineages with hydrogenosomes.