During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1.

Binding Sites Carbon-Sulfur Lyases / genetics Ferredoxins / metabolism Iron-Binding Proteins / metabolism Iron-Sulfur Proteins / metabolism Mitochondrial Proteins / metabolism Saccharomyces cerevisiae / enzymology Saccharomyces cerevisiae Proteins / metabolism Sulfurtransferases / metabolism Frataxin
iron–sulfur protein mitochondria protein complex protein evolution protein–protein interactions

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
02 2022
Historique:
received: 02 12 2021
accepted: 04 01 2022
pubmed: 14 1 2022
medline: 29 4 2022
entrez: 13 1 2022
Statut: ppublish

Résumé

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 accessory FeS cluster biogenesis proteins frataxin (Yfh1) and ferredoxin (Yah1). Yfh1 has been shown to activate cysteine desulfurase enzymatic activity, whereas Yah1 supplies electrons for the persulfide reduction. While Yfh1 interaction with Nfs1 is well understood, the Yah1-Nfs1 interaction is not. Here, based on the results of biochemical experiments involving purified WT and variant proteins, we report that in Saccharomyces cerevisiae, Yah1 and Yfh1 share an evolutionary conserved interaction site on Nfs1. Consistent with this notion, Yah1 and Yfh1 can each 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.

Identifiants

DOI: 10.1016/j.jbc.2022.101570 PMID: 35026224 PMC: PMC8888459
pubmed: 35026224
pii: S0021-9258(22)00010-2
doi: 10.1016/j.jbc.2022.101570
pmc: PMC8888459
pii:
doi:

Substances chimiques

Ferredoxins 0
Iron-Binding Proteins 0
Iron-Sulfur Proteins 0
Mitochondrial Proteins 0
Saccharomyces cerevisiae Proteins 0
Sulfurtransferases EC 2.8.1.-
NFS1 protein, S cerevisiae EC 2.8.1.7
Carbon-Sulfur Lyases EC 4.4.-
cysteine desulfurase EC 4.4.1.-

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

101570

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM127009
Pays : United States

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interests with the content of this article.

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Auteurs

Marta A Uzarska (MA)

Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.

Igor Grochowina (I)

Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.

Joanna Soldek (J)

Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.

Marcin Jelen (M)

Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.

Brenda Schilke (B)

Department of Biochemistry, University of Wisconsin - Madison, Madison, Wisconsin, USA.

Jaroslaw Marszalek (J)

Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland; Department of Biochemistry, University of Wisconsin - Madison, Madison, Wisconsin, USA. Electronic address: jaroslaw.marszalek@ug.edu.pl.

Elizabeth A Craig (EA)

Department of Biochemistry, University of Wisconsin - Madison, Madison, Wisconsin, USA. Electronic address: ecraig@wisc.edu.

Rafal Dutkiewicz (R)

Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland. Electronic address: rafal.dutkiewicz@ug.edu.pl.

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Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Lyases › Carbon-sulfur lyases › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines végétales › Ferrédoxines › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Métalloprotéines › Protéines de liaison au fer › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Métalloprotéines › Protéines de liaison au fer › Protéines à fer non hème › Ferrosulfoprotéines › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines mitochondriales › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › During FeS cluster biogenesis, ferredoxin and...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Sulfur group transferases › Sulfurtransferases › During FeS cluster biogenesis, ferredoxin and...