Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism.
Identifieur interne : 004685 ( Main/Curation ); précédent : 004684; suivant : 004686Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism.
Auteurs : Nicolas Rouhier [France] ; Eric Gelhaye ; Jean Pierre JacquotSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2002.
Descripteurs français
- KwdFr :
- ADN complémentaire (métabolisme), Catalyse (MeSH), Cinétique (MeSH), Clonage moléculaire (MeSH), Cystéine (composition chimique), Dimérisation (MeSH), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Liaison aux protéines (MeSH), Mutagenèse dirigée (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Oxygène (métabolisme), Peroxidases (génétique), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Peroxyde d'hydrogène (composition chimique), Protéines (génétique), Protéines (métabolisme), Protéines recombinantes (métabolisme), Relation dose-effet des médicaments (MeSH), Similitude de séquences d'acides aminés (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Technique de Western (MeSH), Thiols (composition chimique), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- composition chimique : Cystéine, Peroxyde d'hydrogène, Thiols.
- génétique : Peroxidases, Protéines.
- métabolisme : ADN complémentaire, Oxygène, Peroxidases, Protéines, Protéines recombinantes.
- Catalyse, Cinétique, Clonage moléculaire, Dimérisation, Domaine catalytique, Données de séquences moléculaires, Glutarédoxines, Humains, Liaison aux protéines, Mutagenèse dirigée, Mutation, Oxidoreductases, Peroxirédoxines, Relation dose-effet des médicaments, Similitude de séquences d'acides aminés, Structure tertiaire des protéines, Séquence d'acides aminés, Technique de Western, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Blotting, Western (MeSH), Catalysis (MeSH), Catalytic Domain (MeSH), Cloning, Molecular (MeSH), Cysteine (chemistry), DNA, Complementary (metabolism), Dimerization (MeSH), Dose-Response Relationship, Drug (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Hydrogen Peroxide (chemistry), Kinetics (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Oxygen (metabolism), Peroxidases (genetics), Peroxidases (metabolism), Peroxiredoxins (MeSH), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Proteins (genetics), Proteins (metabolism), Recombinant Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Sulfhydryl Compounds (chemistry).
- MESH :
- chemical , chemistry : Cysteine, Hydrogen Peroxide, Sulfhydryl Compounds.
- chemical , genetics : Peroxidases, Proteins.
- chemical , metabolism : DNA, Complementary, Oxygen, Peroxidases, Proteins, Recombinant Proteins.
- Amino Acid Sequence, Blotting, Western, Catalysis, Catalytic Domain, Cloning, Molecular, Dimerization, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Glutaredoxins, Humans, Kinetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Oxidoreductases, Peroxiredoxins, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid.
Abstract
Recently, a poplar phloem peroxiredoxin (Prx) was found to accept both glutaredoxin (Grx) and thioredoxin (Trx) as proton donors. To investigate the catalytic mechanism of the Grx-dependent reduction of hydroperoxides catalyzed by Prx, a series of cysteinic mutants was constructed. Mutation of the most N-terminal conserved cysteine of Prx (Cys-51) demonstrates that it is the catalytic one. The second cysteine (Cys-76) is not essential for peroxiredoxin activity because the C76A mutant retained approximately 25% of the wild type Prx activity. Only one cysteine of the Grx active site (Cys-27) is essential for peroxiredoxin catalysis, indicating that Grx can act in this reaction either via a dithiol or a monothiol pathway. The creation of covalent heterodimers between Prx and Grx mutants confirms that Prx Cys-51 and Grx Cys-27 are the two residues involved in the catalytic mechanism. The integration of a third cysteine in position 152 of the Prx, making it similar in sequence to the Trx-dependent human Prx V, resulted in a protein that had no detectable activity with Grx but kept activity with Trx. Based on these experimental results, a catalytic mechanism is proposed to explain the Grx- and Trx-dependent activities of poplar Prx.
DOI: 10.1074/jbc.M111489200
PubMed: 11832487
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pubmed:11832487Le document en format XML
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<term>Blotting, Western (MeSH)</term>
<term>Catalysis (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Cysteine (chemistry)</term>
<term>DNA, Complementary (metabolism)</term>
<term>Dimerization (MeSH)</term>
<term>Dose-Response Relationship, Drug (MeSH)</term>
<term>Electrophoresis, Polyacrylamide Gel (MeSH)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Hydrogen Peroxide (chemistry)</term>
<term>Kinetics (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Oxygen (metabolism)</term>
<term>Peroxidases (genetics)</term>
<term>Peroxidases (metabolism)</term>
<term>Peroxiredoxins (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Proteins (genetics)</term>
<term>Proteins (metabolism)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Sulfhydryl Compounds (chemistry)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (métabolisme)</term>
<term>Catalyse (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Cystéine (composition chimique)</term>
<term>Dimérisation (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glutarédoxines (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Oxygène (métabolisme)</term>
<term>Peroxidases (génétique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Peroxirédoxines (MeSH)</term>
<term>Peroxyde d'hydrogène (composition chimique)</term>
<term>Protéines (génétique)</term>
<term>Protéines (métabolisme)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Relation dose-effet des médicaments (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Technique de Western (MeSH)</term>
<term>Thiols (composition chimique)</term>
<term>Électrophorèse sur gel de polyacrylamide (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term>
<term>Hydrogen Peroxide</term>
<term>Sulfhydryl Compounds</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term>
<term>Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA, Complementary</term>
<term>Oxygen</term>
<term>Peroxidases</term>
<term>Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term>
<term>Peroxyde d'hydrogène</term>
<term>Thiols</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term>
<term>Protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN complémentaire</term>
<term>Oxygène</term>
<term>Peroxidases</term>
<term>Protéines</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Blotting, Western</term>
<term>Catalysis</term>
<term>Catalytic Domain</term>
<term>Cloning, Molecular</term>
<term>Dimerization</term>
<term>Dose-Response Relationship, Drug</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Glutaredoxins</term>
<term>Humans</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Mutation</term>
<term>Oxidoreductases</term>
<term>Peroxiredoxins</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term>
<term>Cinétique</term>
<term>Clonage moléculaire</term>
<term>Dimérisation</term>
<term>Domaine catalytique</term>
<term>Données de séquences moléculaires</term>
<term>Glutarédoxines</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Mutagenèse dirigée</term>
<term>Mutation</term>
<term>Oxidoreductases</term>
<term>Peroxirédoxines</term>
<term>Relation dose-effet des médicaments</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Technique de Western</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<front><div type="abstract" xml:lang="en">Recently, a poplar phloem peroxiredoxin (Prx) was found to accept both glutaredoxin (Grx) and thioredoxin (Trx) as proton donors. To investigate the catalytic mechanism of the Grx-dependent reduction of hydroperoxides catalyzed by Prx, a series of cysteinic mutants was constructed. Mutation of the most N-terminal conserved cysteine of Prx (Cys-51) demonstrates that it is the catalytic one. The second cysteine (Cys-76) is not essential for peroxiredoxin activity because the C76A mutant retained approximately 25% of the wild type Prx activity. Only one cysteine of the Grx active site (Cys-27) is essential for peroxiredoxin catalysis, indicating that Grx can act in this reaction either via a dithiol or a monothiol pathway. The creation of covalent heterodimers between Prx and Grx mutants confirms that Prx Cys-51 and Grx Cys-27 are the two residues involved in the catalytic mechanism. The integration of a third cysteine in position 152 of the Prx, making it similar in sequence to the Trx-dependent human Prx V, resulted in a protein that had no detectable activity with Grx but kept activity with Trx. Based on these experimental results, a catalytic mechanism is proposed to explain the Grx- and Trx-dependent activities of poplar Prx.</div>
</front>
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<Abstract><AbstractText>Recently, a poplar phloem peroxiredoxin (Prx) was found to accept both glutaredoxin (Grx) and thioredoxin (Trx) as proton donors. To investigate the catalytic mechanism of the Grx-dependent reduction of hydroperoxides catalyzed by Prx, a series of cysteinic mutants was constructed. Mutation of the most N-terminal conserved cysteine of Prx (Cys-51) demonstrates that it is the catalytic one. The second cysteine (Cys-76) is not essential for peroxiredoxin activity because the C76A mutant retained approximately 25% of the wild type Prx activity. Only one cysteine of the Grx active site (Cys-27) is essential for peroxiredoxin catalysis, indicating that Grx can act in this reaction either via a dithiol or a monothiol pathway. The creation of covalent heterodimers between Prx and Grx mutants confirms that Prx Cys-51 and Grx Cys-27 are the two residues involved in the catalytic mechanism. The integration of a third cysteine in position 152 of the Prx, making it similar in sequence to the Trx-dependent human Prx V, resulted in a protein that had no detectable activity with Grx but kept activity with Trx. Based on these experimental results, a catalytic mechanism is proposed to explain the Grx- and Trx-dependent activities of poplar Prx.</AbstractText>
</Abstract>
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<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
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