GlutaredoxinV1, Main, Exploration, bibRecord, 000420

Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.

Identifieur interne : 000420 ( Main/Exploration ); précédent : 000419; suivant : 000421

Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.

Auteurs : Andrew Melber [États-Unis] ; Un Na [États-Unis] ; Ajay Vashisht [États-Unis] ; Benjamin D. Weiler [Allemagne] ; Roland Lill [Allemagne] ; James A. Wohlschlegel [États-Unis] ; Dennis R. Winge [États-Unis]

Source :

eLife [ 2050-084X ] ; 2016.

RBID : pubmed:27532773

Descripteurs français

KwdFr :
- Ferrosulfoprotéines (métabolisme), Mitochondries (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines mitochondriales (génétique), Protéines mitochondriales (métabolisme), Protéome (analyse), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Transport biologique (MeSH).
MESH :
- analyse : Protéome.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Protéines de Saccharomyces cerevisiae, Protéines mitochondriales, Saccharomyces cerevisiae.
- métabolisme : Ferrosulfoprotéines, Mitochondries, Protéines de Saccharomyces cerevisiae, Protéines mitochondriales, Saccharomyces cerevisiae.
- Transport biologique.

English descriptors

KwdEn :
- Biological Transport (MeSH), Iron-Sulfur Proteins (metabolism), Mitochondria (metabolism), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Proteome (analysis), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
MESH :
- chemical , analysis : Proteome.
- chemical , genetics : Mitochondrial Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Iron-Sulfur Proteins, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Mitochondria, Saccharomyces cerevisiae.
- Biological Transport.

Abstract

Iron-sulfur (Fe-S) clusters are essential for many cellular processes, ranging from aerobic respiration, metabolite biosynthesis, ribosome assembly and DNA repair. Mutations in NFU1 and BOLA3 have been linked to genetic diseases with defects in mitochondrial Fe-S centers. Through genetic studies in yeast, we demonstrate that Nfu1 functions in a late step of [4Fe-4S] cluster biogenesis that is of heightened importance during oxidative metabolism. Proteomic studies revealed Nfu1 physical interacts with components of the ISA [4Fe-4S] assembly complex and client proteins that need [4Fe-4S] clusters to function. Additional studies focused on the mitochondrial BolA proteins, Bol1 and Bol3 (yeast homolog to human BOLA3), revealing that Bol1 functions earlier in Fe-S biogenesis with the monothiol glutaredoxin, Grx5, and Bol3 functions late with Nfu1. Given these observations, we propose that Nfu1, assisted by Bol3, functions to facilitate Fe-S transfer from the biosynthetic apparatus to the client proteins preventing oxidative damage to [4Fe-4S] clusters.

DOI: 10.7554/eLife.15991
PubMed: 27532773
PubMed Central: PMC5014551

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondrial Proteins (genetics)</term>
<term>Mitochondrial Proteins (metabolism)</term>
<term>Proteome (analysis)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
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<term>Mitochondries (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines mitochondriales (génétique)</term>
<term>Protéines mitochondriales (métabolisme)</term>
<term>Protéome (analyse)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Transport biologique (MeSH)</term>
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</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Mitochondrial Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Iron-Sulfur Proteins</term>
<term>Mitochondrial Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Protéome</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Iron-sulfur (Fe-S) clusters are essential for many cellular processes, ranging from aerobic respiration, metabolite biosynthesis, ribosome assembly and DNA repair. Mutations in NFU1 and BOLA3 have been linked to genetic diseases with defects in mitochondrial Fe-S centers. Through genetic studies in yeast, we demonstrate that Nfu1 functions in a late step of [4Fe-4S] cluster biogenesis that is of heightened importance during oxidative metabolism. Proteomic studies revealed Nfu1 physical interacts with components of the ISA [4Fe-4S] assembly complex and client proteins that need [4Fe-4S] clusters to function. Additional studies focused on the mitochondrial BolA proteins, Bol1 and Bol3 (yeast homolog to human BOLA3), revealing that Bol1 functions earlier in Fe-S biogenesis with the monothiol glutaredoxin, Grx5, and Bol3 functions late with Nfu1. Given these observations, we propose that Nfu1, assisted by Bol3, functions to facilitate Fe-S transfer from the biosynthetic apparatus to the client proteins preventing oxidative damage to [4Fe-4S] clusters.</div>
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<Abstract><AbstractText>Iron-sulfur (Fe-S) clusters are essential for many cellular processes, ranging from aerobic respiration, metabolite biosynthesis, ribosome assembly and DNA repair. Mutations in NFU1 and BOLA3 have been linked to genetic diseases with defects in mitochondrial Fe-S centers. Through genetic studies in yeast, we demonstrate that Nfu1 functions in a late step of [4Fe-4S] cluster biogenesis that is of heightened importance during oxidative metabolism. Proteomic studies revealed Nfu1 physical interacts with components of the ISA [4Fe-4S] assembly complex and client proteins that need [4Fe-4S] clusters to function. Additional studies focused on the mitochondrial BolA proteins, Bol1 and Bol3 (yeast homolog to human BOLA3), revealing that Bol1 functions earlier in Fe-S biogenesis with the monothiol glutaredoxin, Grx5, and Bol3 functions late with Nfu1. Given these observations, we propose that Nfu1, assisted by Bol3, functions to facilitate Fe-S transfer from the biosynthetic apparatus to the client proteins preventing oxidative damage to [4Fe-4S] clusters.</AbstractText>
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Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.

Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.

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