GlutaredoxinV1, Main, Exploration, bibRecord, 000F84

Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.

Identifieur interne : 000F84 ( Main/Exploration ); précédent : 000F83; suivant : 000F85

Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.

Auteurs : María Teresa Rodríguez-Manzaneque [Espagne] ; Jordi Tamarit ; Gemma Bellí ; Joaquim Ros ; Enrique Herrero

Source :

Molecular biology of the cell [ 1059-1524 ] ; 2002.

RBID : pubmed:11950925

Descripteurs français

KwdFr :
- ADN complémentaire (métabolisme), Antifibrinolytiques (pharmacologie), Données de séquences moléculaires (MeSH), Facteurs temps (MeSH), Fer (métabolisme), Ferrosulfoprotéines (métabolisme), Glutarédoxines (MeSH), Liaison aux protéines (MeSH), Mitochondries (métabolisme), Mutagenèse dirigée (MeSH), Mutation (MeSH), Ménadione (pharmacologie), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Oxygène (métabolisme), Peptides (composition chimique), Plasmides (métabolisme), Protéines (métabolisme), Protéines (physiologie), Saccharomyces cerevisiae (métabolisme), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Technique de Western (MeSH).
MESH :
- composition chimique : Peptides.
- métabolisme : ADN complémentaire, Fer, Ferrosulfoprotéines, Mitochondries, Oxygène, Plasmides, Protéines, Saccharomyces cerevisiae.
- pharmacologie : Antifibrinolytiques, Ménadione.
- physiologie : Protéines.
- Données de séquences moléculaires, Facteurs temps, Glutarédoxines, Liaison aux protéines, Mutagenèse dirigée, Mutation, Oxidoreductases, Oxydoréduction, Structure tertiaire des protéines, Séquence d'acides aminés, Technique de Western.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Antifibrinolytic Agents (pharmacology), Blotting, Western (MeSH), DNA, Complementary (metabolism), Glutaredoxins (MeSH), Iron (metabolism), Iron-Sulfur Proteins (metabolism), Mitochondria (metabolism), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Oxygen (metabolism), Peptides (chemistry), Plasmids (metabolism), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Proteins (metabolism), Proteins (physiology), Saccharomyces cerevisiae (metabolism), Time Factors (MeSH), Vitamin K 3 (pharmacology).
MESH :
- chemical , chemistry : Peptides.
- chemical , metabolism : DNA, Complementary, Iron, Iron-Sulfur Proteins, Oxygen, Proteins.
- chemical , pharmacology : Antifibrinolytic Agents, Vitamin K 3.
- metabolism : Mitochondria, Plasmids, Saccharomyces cerevisiae.
- chemical , physiology : Proteins.
- Amino Acid Sequence, Blotting, Western, Glutaredoxins, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Oxidation-Reduction, Oxidoreductases, Protein Binding, Protein Structure, Tertiary, Time Factors.

Abstract

Yeast cells contain a family of three monothiol glutaredoxins: Grx3, 4, and 5. Absence of Grx5 leads to constitutive oxidative damage, exacerbating that caused by external oxidants. Phenotypic defects associated with the absence of Grx5 are suppressed by overexpression of SSQ1 and ISA2, two genes involved in the synthesis and assembly of iron/sulfur clusters into proteins. Grx5 localizes at the mitochondrial matrix, like other proteins involved in the synthesis of these clusters, and the mature form lacks the first 29 amino acids of the translation product. Absence of Grx5 causes: 1) iron accumulation in the cell, which in turn could promote oxidative damage, and 2) inactivation of enzymes requiring iron/sulfur clusters for their activity. Reduction of iron levels in grx5 null mutants does not restore the activity of iron/sulfur enzymes, and cell growth defects are not suppressed in anaerobiosis or in the presence of disulfide reductants. Hence, Grx5 forms part of the mitochondrial machinery involved in the synthesis and assembly of iron/sulfur centers.

DOI: 10.1091/mbc.01-10-0517
PubMed: 11950925
PubMed Central: PMC102255

Affiliations:

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

to stream Main, to step Corpus: 000F83
to stream Main, to step Curation: 000F83

Le document en format XML

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<term>DNA, Complementary (metabolism)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Iron (metabolism)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Mitochondria (metabolism)</term>
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<term>Oxygen (metabolism)</term>
<term>Peptides (chemistry)</term>
<term>Plasmids (metabolism)</term>
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<front><div type="abstract" xml:lang="en">Yeast cells contain a family of three monothiol glutaredoxins: Grx3, 4, and 5. Absence of Grx5 leads to constitutive oxidative damage, exacerbating that caused by external oxidants. Phenotypic defects associated with the absence of Grx5 are suppressed by overexpression of SSQ1 and ISA2, two genes involved in the synthesis and assembly of iron/sulfur clusters into proteins. Grx5 localizes at the mitochondrial matrix, like other proteins involved in the synthesis of these clusters, and the mature form lacks the first 29 amino acids of the translation product. Absence of Grx5 causes: 1) iron accumulation in the cell, which in turn could promote oxidative damage, and 2) inactivation of enzymes requiring iron/sulfur clusters for their activity. Reduction of iron levels in grx5 null mutants does not restore the activity of iron/sulfur enzymes, and cell growth defects are not suppressed in anaerobiosis or in the presence of disulfide reductants. Hence, Grx5 forms part of the mitochondrial machinery involved in the synthesis and assembly of iron/sulfur centers.</div>
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<Abstract><AbstractText>Yeast cells contain a family of three monothiol glutaredoxins: Grx3, 4, and 5. Absence of Grx5 leads to constitutive oxidative damage, exacerbating that caused by external oxidants. Phenotypic defects associated with the absence of Grx5 are suppressed by overexpression of SSQ1 and ISA2, two genes involved in the synthesis and assembly of iron/sulfur clusters into proteins. Grx5 localizes at the mitochondrial matrix, like other proteins involved in the synthesis of these clusters, and the mature form lacks the first 29 amino acids of the translation product. Absence of Grx5 causes: 1) iron accumulation in the cell, which in turn could promote oxidative damage, and 2) inactivation of enzymes requiring iron/sulfur clusters for their activity. Reduction of iron levels in grx5 null mutants does not restore the activity of iron/sulfur enzymes, and cell growth defects are not suppressed in anaerobiosis or in the presence of disulfide reductants. Hence, Grx5 forms part of the mitochondrial machinery involved in the synthesis and assembly of iron/sulfur centers.</AbstractText>
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Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.

Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.

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