PoplarV1, Main, Exploration, bibRecord, 003971

Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.

Identifieur interne : 003971 ( Main/Exploration ); précédent : 003970; suivant : 003972

Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.

Auteurs : Sibali Bandyopadhyay [États-Unis] ; Filipe Gama ; Maria Micaela Molina-Navarro ; José Manuel Gualberto ; Ronald Claxton ; Sunil G. Naik ; Boi Hanh Huynh ; Enrique Herrero ; Jean Pierre Jacquot ; Michael K. Johnson ; Nicolas Rouhier

Source :

The EMBO journal [ 1460-2075 ] ; 2008.

RBID : pubmed:18354500

Descripteurs français

KwdFr :
- Analyse spectrale Raman (MeSH), Apoprotéines (métabolisme), Arabidopsis (enzymologie), Chloroplastes (enzymologie), Cinétique (MeSH), Dichroïsme circulaire (MeSH), Données de séquences moléculaires (MeSH), Facteurs temps (MeSH), Ferrosulfoprotéines (isolement et purification), Ferrosulfoprotéines (métabolisme), Ferrédoxines (métabolisme), Fractions subcellulaires (enzymologie), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Modèles biologiques (MeSH), Mutation (génétique), Populus (enzymologie), Protéines d'Arabidopsis (MeSH), Saccharomyces cerevisiae (métabolisme), Sites de fixation (MeSH), Spectrophotométrie UV (MeSH), Spectroscopie Mossbauer (MeSH), Séquence d'acides aminés (MeSH), Test de complémentation (MeSH), Thiols (métabolisme), Transport des protéines (MeSH).
MESH :
- composition chimique : Glutarédoxines.
- enzymologie : Arabidopsis, Chloroplastes, Fractions subcellulaires, Populus.
- génétique : Mutation.
- isolement et purification : Ferrosulfoprotéines.
- métabolisme : Apoprotéines, Ferrosulfoprotéines, Ferrédoxines, Glutarédoxines, Saccharomyces cerevisiae, Thiols.
- Analyse spectrale Raman, Cinétique, Dichroïsme circulaire, Données de séquences moléculaires, Facteurs temps, Modèles biologiques, Protéines d'Arabidopsis, Sites de fixation, Spectrophotométrie UV, Spectroscopie Mossbauer, Séquence d'acides aminés, Test de complémentation, Transport des protéines.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Apoproteins (metabolism), Arabidopsis (enzymology), Arabidopsis Proteins (MeSH), Binding Sites (MeSH), Chloroplasts (enzymology), Circular Dichroism (MeSH), Ferredoxins (metabolism), Genetic Complementation Test (MeSH), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Iron-Sulfur Proteins (isolation & purification), Iron-Sulfur Proteins (metabolism), Kinetics (MeSH), Models, Biological (MeSH), Molecular Sequence Data (MeSH), Mutation (genetics), Populus (enzymology), Protein Transport (MeSH), Saccharomyces cerevisiae (metabolism), Spectrophotometry, Ultraviolet (MeSH), Spectroscopy, Mossbauer (MeSH), Spectrum Analysis, Raman (MeSH), Subcellular Fractions (enzymology), Sulfhydryl Compounds (metabolism), Time Factors (MeSH).
MESH :
- chemical , chemistry : Glutaredoxins.
- chemical , isolation & purification : Iron-Sulfur Proteins.
- chemical , metabolism : Apoproteins, Ferredoxins, Glutaredoxins, Iron-Sulfur Proteins, Sulfhydryl Compounds.
- enzymology : Arabidopsis, Chloroplasts, Populus, Subcellular Fractions.
- genetics : Mutation.
- metabolism : Saccharomyces cerevisiae.
- Amino Acid Sequence, Arabidopsis Proteins, Binding Sites, Circular Dichroism, Genetic Complementation Test, Kinetics, Models, Biological, Molecular Sequence Data, Protein Transport, Spectrophotometry, Ultraviolet, Spectroscopy, Mossbauer, Spectrum Analysis, Raman, Time Factors.

Abstract

Glutaredoxins (Grxs) are small oxidoreductases that reduce disulphide bonds or protein-glutathione mixed disulphides. More than 30 distinct grx genes are expressed in higher plants, but little is currently known concerning their functional diversity. This study presents biochemical and spectroscopic evidence for incorporation of a [2Fe-2S] cluster in two heterologously expressed chloroplastic Grxs, GrxS14 and GrxS16, and in vitro cysteine desulphurase-mediated assembly of an identical [2Fe-2S] cluster in apo-GrxS14. These Grxs possess the same monothiol CGFS active site as yeast Grx5 and both were able to complement a yeast grx5 mutant defective in Fe-S cluster assembly. In vitro kinetic studies monitored by CD spectroscopy indicate that [2Fe-2S] clusters on GrxS14 are rapidly and quantitatively transferred to apo chloroplast ferredoxin. These data demonstrate that chloroplast CGFS Grxs have the potential to function as scaffold proteins for the assembly of [2Fe-2S] clusters that can be transferred intact to physiologically relevant acceptor proteins. Alternatively, they may function in the storage and/or delivery of preformed Fe-S clusters or in the regulation of the chloroplastic Fe-S cluster assembly machinery.

DOI: 10.1038/emboj.2008.50
PubMed: 18354500
PubMed Central: PMC2323258

Affiliations:

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

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Le document en format XML

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<term>Arabidopsis Proteins (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Chloroplasts (enzymology)</term>
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<term>Genetic Complementation Test (MeSH)</term>
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<term>Models, Biological (MeSH)</term>
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<term>Mutation (genetics)</term>
<term>Populus (enzymology)</term>
<term>Protein Transport (MeSH)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Spectrophotometry, Ultraviolet (MeSH)</term>
<term>Spectroscopy, Mossbauer (MeSH)</term>
<term>Spectrum Analysis, Raman (MeSH)</term>
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<term>Time Factors (MeSH)</term>
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<term>Protéines d'Arabidopsis (MeSH)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Spectrophotométrie UV (MeSH)</term>
<term>Spectroscopie Mossbauer (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Test de complémentation (MeSH)</term>
<term>Thiols (métabolisme)</term>
<term>Transport des protéines (MeSH)</term>
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<term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
<term>Sulfhydryl Compounds</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term>
<term>Chloroplastes</term>
<term>Fractions subcellulaires</term>
<term>Populus</term>
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<term>Chloroplasts</term>
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<term>Données de séquences moléculaires</term>
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<term>Protéines d'Arabidopsis</term>
<term>Sites de fixation</term>
<term>Spectrophotométrie UV</term>
<term>Spectroscopie Mossbauer</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are small oxidoreductases that reduce disulphide bonds or protein-glutathione mixed disulphides. More than 30 distinct grx genes are expressed in higher plants, but little is currently known concerning their functional diversity. This study presents biochemical and spectroscopic evidence for incorporation of a [2Fe-2S] cluster in two heterologously expressed chloroplastic Grxs, GrxS14 and GrxS16, and in vitro cysteine desulphurase-mediated assembly of an identical [2Fe-2S] cluster in apo-GrxS14. These Grxs possess the same monothiol CGFS active site as yeast Grx5 and both were able to complement a yeast grx5 mutant defective in Fe-S cluster assembly. In vitro kinetic studies monitored by CD spectroscopy indicate that [2Fe-2S] clusters on GrxS14 are rapidly and quantitatively transferred to apo chloroplast ferredoxin. These data demonstrate that chloroplast CGFS Grxs have the potential to function as scaffold proteins for the assembly of [2Fe-2S] clusters that can be transferred intact to physiologically relevant acceptor proteins. Alternatively, they may function in the storage and/or delivery of preformed Fe-S clusters or in the regulation of the chloroplastic Fe-S cluster assembly machinery.</div>
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<ArticleTitle>Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.</ArticleTitle>
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<Abstract><AbstractText>Glutaredoxins (Grxs) are small oxidoreductases that reduce disulphide bonds or protein-glutathione mixed disulphides. More than 30 distinct grx genes are expressed in higher plants, but little is currently known concerning their functional diversity. This study presents biochemical and spectroscopic evidence for incorporation of a [2Fe-2S] cluster in two heterologously expressed chloroplastic Grxs, GrxS14 and GrxS16, and in vitro cysteine desulphurase-mediated assembly of an identical [2Fe-2S] cluster in apo-GrxS14. These Grxs possess the same monothiol CGFS active site as yeast Grx5 and both were able to complement a yeast grx5 mutant defective in Fe-S cluster assembly. In vitro kinetic studies monitored by CD spectroscopy indicate that [2Fe-2S] clusters on GrxS14 are rapidly and quantitatively transferred to apo chloroplast ferredoxin. These data demonstrate that chloroplast CGFS Grxs have the potential to function as scaffold proteins for the assembly of [2Fe-2S] clusters that can be transferred intact to physiologically relevant acceptor proteins. Alternatively, they may function in the storage and/or delivery of preformed Fe-S clusters or in the regulation of the chloroplastic Fe-S cluster assembly machinery.</AbstractText>
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Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.

Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.

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