PXD029519

PXD029519 is an original dataset announced via ProteomeXchange.

Title	Overlapping binding site for ferredoxin and frataxin on yeast cysteine desulfurase participating in FeS cluster biogenesis
Description	In mitochondria cysteine desulfurase (Nfs1) plays a central role in the biosynthesis of iron-sulfur (FeS) clusters, cofactors critical for activity of many cellular proteins. Nfs1 functions both as a sulfur donor for cluster assembly and as a binding platform for other proteins functioning in the process. These include, not only the dedicated scaffold protein (Isu1) on which FeS clusters are synthesized, but also frataxin (Yfh1) and ferredoxin (Yah1). Yfh1 activates cysteine desulfurase enzymatic activity, while Yah1 supplies electrons for persulfide reduction. Yfh1 interaction with Nfs1 is well understood; that of Yah1 is not. Here, based on the results of biochemical experiments involving purified wild-type and variant proteins, we report that in Saccharomyces cerevisiae Yah1 and Yfh1 share an evolutionary conserved interaction site on Nfs1. Consistent with this notion each can displace the other from Nfs1, but are inefficient competitors when a variant with an altered interaction site is used. Thus, the binding mode of Yah1 and Yfh1 interacting with Nfs1 in mitochondria of S. cerevisiae resembles the mutually exclusive binding of ferredoxin and frataxin with cysteine desulfurase reported for the bacterial FeS cluster assembly system. Our findings are consistent with the generally accepted scenario that the mitochondrial FeS cluster assembly system was inherited from bacterial ancestors of mitochondria.
HostingRepository	PRIDE
AnnounceDate	2022-05-25
AnnouncementXML	Submission_2022-05-25_09:10:08.500.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD029519
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Igor Grochowina
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2021-11-02 07:23:56	ID requested
⏵ 1	2022-05-25 09:10:09	announced

Uzarska MA, Grochowina I, Soldek J, Jelen M, Schilke B, Marszalek J, Craig EA, Dutkiewicz R, During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1. J Biol Chem, 298(2):101570(2022) [pubmed]

submitter keyword: iron-sulfur protein, protein complex, LC-MSMS

Jaroslaw Marszalek
contact affiliation	Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, 58 Abrahama St., 80-307 Gdansk, Poland
contact email	jaroslaw.marszalek@ug.edu.pl
lab head
Igor Grochowina
contact affiliation	University of Gdansk
contact email	igor.grochowina@phdstud.ug.edu.pl
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD029519
     1. Label: PRIDE project
     2. Name: Overlapping binding site for ferredoxin and frataxin on yeast cysteine desulfurase participating in FeS cluster biogenesis