GlutaredoxinV1, Main, Exploration, bibRecord, 000905

The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group.

Identifieur interne : 000905 ( Main/Exploration ); précédent : 000904; suivant : 000906

The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group.

Auteurs : Bastian Hoffmann [Allemagne] ; Marta A. Uzarska ; Carsten Berndt ; José R. Godoy ; Petra Haunhorst ; Christopher Horst Lillig ; Roland Lill ; Ulrich Mühlenhoff

Source :

Antioxidants & redox signaling [ 1557-7716 ] ; 2011.

RBID : pubmed:21299470

Descripteurs français

English descriptors

KwdEn :
- Catalytic Domain (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Protein Structure, Tertiary (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Schizosaccharomyces (genetics), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Thioredoxins (genetics), Thioredoxins (metabolism).
MESH :
- chemical , genetics : Glutaredoxins, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Thioredoxins.
- chemical , metabolism : Glutaredoxins, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Thioredoxins.
- genetics : Saccharomyces cerevisiae, Schizosaccharomyces.
- metabolism : Saccharomyces cerevisiae, Schizosaccharomyces.
- Catalytic Domain, Protein Structure, Tertiary.

Abstract

Monothiol glutaredoxins (Grxs) with a noncanonical CGFS active site are found in all kingdoms of life. They include members with a single domain and thioredoxin-Grx fusion proteins. In Saccharomyces cerevisiae, the multidomain Grx3 and Grx4 play an essential role in intracellular iron trafficking. This crucial task is mediated by an essential Fe/S cofactor. This study shows that this unique physiological role cannot be executed by single domain Grxs, because the thioredoxin domain is indispensable for function in vivo. Mutational analysis revealed that a CPxS active site motif is fully compatible with Fe/S cluster binding on Grx4, while a dithiol active site results in cofactor destabilization and a moderate impairment of in vivo function. These requirements for Fe/S cofactor stabilization on Grx4 are virtually the opposite of those previously reported for single domain Grxs. Grx4 functions as iron sensor for the iron-sensing transcription factor Aft1 in S. cerevisiae. We found that Aft1 binds to a conserved binding site at the C-terminus of Grx4. This interaction is essential for the regulation of Aft1. Collectively, our analysis demonstrates that the multidomain monothiol Grxs form a unique protein family distinct from that of the single domain Grxs.

DOI: 10.1089/ars.2010.3811
PubMed: 21299470

Affiliations:

Allemagne

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Le document en format XML

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<series><title level="j">Antioxidants & redox signaling</title>
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<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Schizosaccharomyces (genetics)</term>
<term>Schizosaccharomyces (metabolism)</term>
<term>Schizosaccharomyces pombe Proteins (genetics)</term>
<term>Schizosaccharomyces pombe Proteins (metabolism)</term>
<term>Thioredoxins (genetics)</term>
<term>Thioredoxins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Domaine catalytique (MeSH)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de Schizosaccharomyces pombe (génétique)</term>
<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Schizosaccharomyces (génétique)</term>
<term>Schizosaccharomyces (métabolisme)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Thiorédoxines (génétique)</term>
<term>Thiorédoxines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Schizosaccharomyces pombe Proteins</term>
<term>Thioredoxins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Schizosaccharomyces pombe Proteins</term>
<term>Thioredoxins</term>
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<term>Schizosaccharomyces</term>
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<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de Schizosaccharomyces pombe</term>
<term>Saccharomyces cerevisiae</term>
<term>Schizosaccharomyces</term>
<term>Thiorédoxines</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
<term>Schizosaccharomyces</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de Schizosaccharomyces pombe</term>
<term>Saccharomyces cerevisiae</term>
<term>Schizosaccharomyces</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term>
<term>Protein Structure, Tertiary</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Domaine catalytique</term>
<term>Structure tertiaire des protéines</term>
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<front><div type="abstract" xml:lang="en">Monothiol glutaredoxins (Grxs) with a noncanonical CGFS active site are found in all kingdoms of life. They include members with a single domain and thioredoxin-Grx fusion proteins. In Saccharomyces cerevisiae, the multidomain Grx3 and Grx4 play an essential role in intracellular iron trafficking. This crucial task is mediated by an essential Fe/S cofactor. This study shows that this unique physiological role cannot be executed by single domain Grxs, because the thioredoxin domain is indispensable for function in vivo. Mutational analysis revealed that a CPxS active site motif is fully compatible with Fe/S cluster binding on Grx4, while a dithiol active site results in cofactor destabilization and a moderate impairment of in vivo function. These requirements for Fe/S cofactor stabilization on Grx4 are virtually the opposite of those previously reported for single domain Grxs. Grx4 functions as iron sensor for the iron-sensing transcription factor Aft1 in S. cerevisiae. We found that Aft1 binds to a conserved binding site at the C-terminus of Grx4. This interaction is essential for the regulation of Aft1. Collectively, our analysis demonstrates that the multidomain monothiol Grxs form a unique protein family distinct from that of the single domain Grxs.</div>
</front>
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<Abstract><AbstractText>Monothiol glutaredoxins (Grxs) with a noncanonical CGFS active site are found in all kingdoms of life. They include members with a single domain and thioredoxin-Grx fusion proteins. In Saccharomyces cerevisiae, the multidomain Grx3 and Grx4 play an essential role in intracellular iron trafficking. This crucial task is mediated by an essential Fe/S cofactor. This study shows that this unique physiological role cannot be executed by single domain Grxs, because the thioredoxin domain is indispensable for function in vivo. Mutational analysis revealed that a CPxS active site motif is fully compatible with Fe/S cluster binding on Grx4, while a dithiol active site results in cofactor destabilization and a moderate impairment of in vivo function. These requirements for Fe/S cofactor stabilization on Grx4 are virtually the opposite of those previously reported for single domain Grxs. Grx4 functions as iron sensor for the iron-sensing transcription factor Aft1 in S. cerevisiae. We found that Aft1 binds to a conserved binding site at the C-terminus of Grx4. This interaction is essential for the regulation of Aft1. Collectively, our analysis demonstrates that the multidomain monothiol Grxs form a unique protein family distinct from that of the single domain Grxs.</AbstractText>
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	Serveur d'exploration sur la glutarédoxine
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Serveur d'exploration sur la glutarédoxine

The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group.

The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group.

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