Evidence map›Paper›PMID 35026224›Full record

ArticleThe Journal of biological chemistry2022

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

Marta A Uzarska, Igor Grochowina, Joanna Soldek, Marcin Jelen, Brenda Schilke, Jaroslaw Marszalek, Elizabeth A Craig, Rafal Dutkiewicz

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 17 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Marta A UzarskaIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.
Igor GrochowinaIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.
Joanna SoldekIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.
Marcin JelenIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland.
Brenda SchilkeDepartment of Biochemistry, University of Wisconsin - Madison, Madison, Wisconsin, USA.
Jaroslaw MarszalekIntercollegiate 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 CraigDepartment of Biochemistry, University of Wisconsin - Madison, Madison, Wisconsin, USA. Electronic address: ecraig@wisc.edu.
Rafal DutkiewiczIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdansk, Poland. Electronic address: rafal.dutkiewicz@ug.edu.pl.
Gdańsk Medical University · PLUniversity of Wisconsin–Madison · USUniversity of Gdańsk · PL

Funding

Functional diversity of Hsp70 and J-protein chaperone systemsR35GM127009 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ELIZABETH A · 2018 to 2022
$1.9M
NIGMS NIH HHS R35 GM127009
6 · The paper itself

Abstract

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.

Indexed as

FerredoxinsIron-Sulfur ProteinsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsSulfurtransferasesBinding SitesCarbon-Sulfur LyasesFrataxinIron-Binding ProteinsSaccharomyces cerevisiaeCarbon-Sulfur Lyasescysteine desulfuraseFerredoxinsFrataxinIron-Binding ProteinsIron-Sulfur ProteinsMitochondrial ProteinsNFS1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSulfurtransferasesiron–sulfur proteinmitochondriaprotein complexprotein evolutionprotein–protein interactions

Identifiers

PMID35026224
PMCPMC8888459
OpenAlexW4206694885

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.