GlutaredoxinV1, Main, Exploration, bibRecord, 000703

The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.

Identifieur interne : 000703 ( Main/Exploration ); précédent : 000702; suivant : 000704

The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.

Auteurs : Marta A. Uzarska [Allemagne] ; Rafal Dutkiewicz ; Sven-Andreas Freibert ; Roland Lill ; Ulrich Mühlenhoff

Source :

Molecular biology of the cell [ 1939-4586 ] ; 2013.

RBID : pubmed:23615440

Descripteurs français

English descriptors

Abstract

The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Similar to its bacterial orthologue HscA, Ssq1 binds to the scaffold protein Isu1, thereby facilitating dissociation of the newly synthesized Fe/S cluster on Isu1 and its transfer to target apoproteins. Here we use in vivo and in vitro approaches to show that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. Grx5 binding does not stimulate the ATPase activity of Ssq1 and is most pronounced for the ADP-bound form of Ssq1, which interacts with Isu1 most tightly. The vicinity of Isu1 and Grx5 on the Hsp70 chaperone facilitates rapid Fe/S cluster transfer from Isu1 to Grx5. Grx5 and its bound Fe/S cluster are required for maturation of all cellular Fe/S proteins, regardless of the type of bound Fe/S cofactor and subcellular localization. Hence Grx5 functions as a late-acting component of the core Fe/S cluster (ISC) assembly machinery linking the Fe/S cluster synthesis reaction on Isu1 with late assembly steps involving Fe/S cluster targeting to dedicated apoproteins.

DOI: 10.1091/mbc.E12-09-0644
PubMed: 23615440
PubMed Central: PMC3681689

Affiliations:

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Le document en format XML

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<term>Adenosine Triphosphate (metabolism)</term>
<term>Binding Sites (MeSH)</term>
<term>Cytosol (metabolism)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>HSP70 Heat-Shock Proteins (genetics)</term>
<term>HSP70 Heat-Shock Proteins (metabolism)</term>
<term>Immunoprecipitation (MeSH)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondrial Proteins (genetics)</term>
<term>Mitochondrial Proteins (metabolism)</term>
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<term>Molecular Chaperones (metabolism)</term>
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<term>Protein Binding (MeSH)</term>
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<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
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<term>Adénosine triphosphate (métabolisme)</term>
<term>Chaperons moléculaires (génétique)</term>
<term>Chaperons moléculaires (métabolisme)</term>
<term>Cytosol (métabolisme)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
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<term>Liaison aux protéines (MeSH)</term>
<term>Mitochondries (métabolisme)</term>
<term>Mutation (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines du choc thermique HSP70 (génétique)</term>
<term>Protéines du choc thermique HSP70 (métabolisme)</term>
<term>Protéines mitochondriales (génétique)</term>
<term>Protéines mitochondriales (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Électrophorèse sur gel de polyacrylamide (MeSH)</term>
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<term>Iron-Sulfur Proteins</term>
<term>Mitochondrial Proteins</term>
<term>Molecular Chaperones</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<term>HSP70 Heat-Shock Proteins</term>
<term>Iron-Sulfur Proteins</term>
<term>Mitochondrial Proteins</term>
<term>Molecular Chaperones</term>
<term>Saccharomyces cerevisiae Proteins</term>
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<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines du choc thermique HSP70</term>
<term>Protéines mitochondriales</term>
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<term>Mitochondria</term>
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<term>Adénosine triphosphate</term>
<term>Chaperons moléculaires</term>
<term>Cytosol</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Mitochondries</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines du choc thermique HSP70</term>
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<front><div type="abstract" xml:lang="en">The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Similar to its bacterial orthologue HscA, Ssq1 binds to the scaffold protein Isu1, thereby facilitating dissociation of the newly synthesized Fe/S cluster on Isu1 and its transfer to target apoproteins. Here we use in vivo and in vitro approaches to show that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. Grx5 binding does not stimulate the ATPase activity of Ssq1 and is most pronounced for the ADP-bound form of Ssq1, which interacts with Isu1 most tightly. The vicinity of Isu1 and Grx5 on the Hsp70 chaperone facilitates rapid Fe/S cluster transfer from Isu1 to Grx5. Grx5 and its bound Fe/S cluster are required for maturation of all cellular Fe/S proteins, regardless of the type of bound Fe/S cofactor and subcellular localization. Hence Grx5 functions as a late-acting component of the core Fe/S cluster (ISC) assembly machinery linking the Fe/S cluster synthesis reaction on Isu1 with late assembly steps involving Fe/S cluster targeting to dedicated apoproteins.</div>
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<Abstract><AbstractText>The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Similar to its bacterial orthologue HscA, Ssq1 binds to the scaffold protein Isu1, thereby facilitating dissociation of the newly synthesized Fe/S cluster on Isu1 and its transfer to target apoproteins. Here we use in vivo and in vitro approaches to show that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. Grx5 binding does not stimulate the ATPase activity of Ssq1 and is most pronounced for the ADP-bound form of Ssq1, which interacts with Isu1 most tightly. The vicinity of Isu1 and Grx5 on the Hsp70 chaperone facilitates rapid Fe/S cluster transfer from Isu1 to Grx5. Grx5 and its bound Fe/S cluster are required for maturation of all cellular Fe/S proteins, regardless of the type of bound Fe/S cofactor and subcellular localization. Hence Grx5 functions as a late-acting component of the core Fe/S cluster (ISC) assembly machinery linking the Fe/S cluster synthesis reaction on Isu1 with late assembly steps involving Fe/S cluster targeting to dedicated apoproteins.</AbstractText>
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The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.

The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.

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