PXD019551

PXD019551 is an original dataset announced via ProteomeXchange.

Title	Drosophila NFS1.R77 is required for differential protein complex composition
Description	S-adenosylmethionine (SAM) is the principle biological methyl group donor for a diverse range of substrates. It is synthesised in the cytosolic methionine cycle and shuttled throughout the cell. The mitochondrial SAM (mitoSAM) pool depends on import through the inner-membrane SAMC and supports the maturation of metabolites and mitochondrial RNAs. We demonstrated that mitoSAM differentially effects mitochondrial function. Metabolite and iron-sulphur cluster biosynthesis are disrupted due to acutely decreased methylation potential, while prolonged mitoSAM deficiency affects fly longevity and OXPHOS stability. We developed a fly-compatible SILAC labelling technique and mapped mitochondrial protein methylation sites. Based on a novel mono-methylation on the DmR77 (HsR72) of the cysteine desulfurase NFS1 our data indicates that methylation can be used to regulate differential protein complex composition in mitochondria on the basis of immunoprecipitation data in this submission. While iron-sulphur cluster containing proteins enriched with Drosophila Nfs1.R77F that mimics a constitutively methylated Nfs1, the iron sequestering protein Fer1HCH bound stronger to Nfs1.R77K that resembles absence of methylation. Our results define the critical role of cytoplasmic SAM production for mitochondrial methylation events and highlight the indirect effect of one-carbon metabolism on cellular bioenergetics.
HostingRepository	PRIDE
AnnounceDate	2021-02-22
AnnouncementXML	Submission_2021-02-21_23:00:19.804.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Florian Schober
SpeciesList	scientific name: Drosophila melanogaster (Fruit fly); NCBI TaxID: 7227;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2020-06-03 17:13:46	ID requested
⏵ 1	2021-02-21 23:00:20	announced

Rosenberger FA, Moore D, Atanassov I, Moedas MF, Clemente P, V, é, gv, á, ri Á, Fissi NE, Filograna R, Bucher AL, Hinze Y, The M, Hedman E, Chernogubova E, Begzati A, Wibom R, Jain M, Nilsson R, K, ä, ll L, Wedell A, Freyer C, Wredenberg A, The one-carbon pool controls mitochondrial energy metabolism via complex I and iron-sulfur clusters. Sci Adv, 7(8):(2021) [pubmed]

submitter keyword: Drosophila, NFS1, iron sulphur clusters

Anna Wredenberg
contact affiliation	Department of Medical Biochemisty and Biophysics, Karolinska Institute, Sweden
contact email	anna.wredenberg@ki.se
lab head
Florian Schober
contact affiliation	MMK, Karolinska Institute
contact email	florian.schober@ki.se
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/2021/02/PXD019551

PRIDE project URI

• PRIDE
  1. PXD019551
     1. Label: PRIDE project
     2. Name: Drosophila NFS1.R77 is required for differential protein complex composition