PoplarV1, Main, Exploration, bibRecord, 004326

A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase.

Identifieur interne : 004326 ( Main/Exploration ); précédent : 004325; suivant : 004327

A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase.

Auteurs : Eric Gelhaye [France] ; Nicolas Rouhier ; Joelle Gérard ; Yves Jolivet ; José Gualberto ; Nicolas Navrot ; Per-Ingvard Ohlsson ; Gunnar Wingsle ; Masakazu Hirasawa ; David B. Knaff ; Hongmei Wang ; Pierre Dizengremel ; Yves Meyer ; Jean-Pierre Jacquot

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.

RBID : pubmed:15385674

Descripteurs français

English descriptors

KwdEn :
- Base Sequence (MeSH), DNA, Recombinant (genetics), Glutathione Peroxidase (metabolism), Mitochondria (metabolism), Mitochondrial Proteins (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Phylogeny (MeSH), Plant Proteins (genetics), Plant Proteins (metabolism), Plants (genetics), Plants (metabolism), Plants, Genetically Modified (MeSH), Populus (genetics), Populus (metabolism), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Thioredoxin h (MeSH).
MESH :
- chemical , genetics : DNA, Recombinant, Plant Proteins, Recombinant Fusion Proteins.
- chemical , metabolism : Glutathione Peroxidase, Oxidoreductases, Plant Proteins, Recombinant Fusion Proteins.
- genetics : Plants, Populus.
- metabolism : Mitochondria, Plants, Populus.
- Base Sequence, Mitochondrial Proteins, Oxidation-Reduction, Phylogeny, Plants, Genetically Modified, Thioredoxin h.

Abstract

The plant mitochondrial thioredoxin (Trx) system has been described as containing an NADPH-dependent Trx reductase and Trx o. In addition to the mitochondrial isoform, Trx o, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx h isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrxh2) belonging to the Trx h group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrxh2 is targeted to plant mitochondria. The recombinant protein, PtTrxh2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrxh2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrxh2 nor AtTrxo1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrxh2 with glutathione disulfide led to the formation of glutathionylated Trx, identified by mass spectrometry. The formation of a glutathione adduct increases the redox potential of PtTrxh2 from -290 to -225 mV. In addition to Trx o, this study shows that Trx h could also be present in mitochondria. This previously unrecognized complexity is not unexpected, considering the multiple redox-regulated processes found in plant mitochondria.

DOI: 10.1073/pnas.0405282101
PubMed: 15385674
PubMed Central: PMC521959

Affiliations:

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

to stream Main, to step Corpus: 004199
to stream Main, to step Curation: 004199

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term>
<term>DNA, Recombinant (genetics)</term>
<term>Glutathione Peroxidase (metabolism)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondrial Proteins (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Phylogeny (MeSH)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Plants (genetics)</term>
<term>Plants (metabolism)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Populus (genetics)</term>
<term>Populus (metabolism)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Thioredoxin h (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>ADN recombiné (génétique)</term>
<term>Glutathione peroxidase (métabolisme)</term>
<term>Mitochondries (métabolisme)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Phylogenèse (MeSH)</term>
<term>Plantes (génétique)</term>
<term>Plantes (métabolisme)</term>
<term>Populus (génétique)</term>
<term>Populus (métabolisme)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines mitochondriales (MeSH)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Thiorédoxine h (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Recombinant</term>
<term>Plant Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione Peroxidase</term>
<term>Oxidoreductases</term>
<term>Plant Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plants</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN recombiné</term>
<term>Plantes</term>
<term>Populus</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term>
<term>Plants</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathione peroxidase</term>
<term>Mitochondries</term>
<term>Oxidoreductases</term>
<term>Plantes</term>
<term>Populus</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term>
<term>Mitochondrial Proteins</term>
<term>Oxidation-Reduction</term>
<term>Phylogeny</term>
<term>Plants, Genetically Modified</term>
<term>Thioredoxin h</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term>
<term>Phylogenèse</term>
<term>Protéines mitochondriales</term>
<term>Séquence nucléotidique</term>
<term>Thiorédoxine h</term>
<term>Végétaux génétiquement modifiés</term>
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<front><div type="abstract" xml:lang="en">The plant mitochondrial thioredoxin (Trx) system has been described as containing an NADPH-dependent Trx reductase and Trx o. In addition to the mitochondrial isoform, Trx o, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx h isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrxh2) belonging to the Trx h group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrxh2 is targeted to plant mitochondria. The recombinant protein, PtTrxh2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrxh2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrxh2 nor AtTrxo1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrxh2 with glutathione disulfide led to the formation of glutathionylated Trx, identified by mass spectrometry. The formation of a glutathione adduct increases the redox potential of PtTrxh2 from -290 to -225 mV. In addition to Trx o, this study shows that Trx h could also be present in mitochondria. This previously unrecognized complexity is not unexpected, considering the multiple redox-regulated processes found in plant mitochondria.</div>
</front>
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<DateCompleted><Year>2004</Year>
<Month>11</Month>
<Day>04</Day>
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<ArticleTitle>A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase.</ArticleTitle>
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<Abstract><AbstractText>The plant mitochondrial thioredoxin (Trx) system has been described as containing an NADPH-dependent Trx reductase and Trx o. In addition to the mitochondrial isoform, Trx o, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx h isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrxh2) belonging to the Trx h group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrxh2 is targeted to plant mitochondria. The recombinant protein, PtTrxh2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrxh2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrxh2 nor AtTrxo1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrxh2 with glutathione disulfide led to the formation of glutathionylated Trx, identified by mass spectrometry. The formation of a glutathione adduct increases the redox potential of PtTrxh2 from -290 to -225 mV. In addition to Trx o, this study shows that Trx h could also be present in mitochondria. This previously unrecognized complexity is not unexpected, considering the multiple redox-regulated processes found in plant mitochondria.</AbstractText>
</Abstract>
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<ForeName>Eric</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Unité Mixte de Recherche, Institut National de la Recherche Agronomique 1136, Interactions Arbres/Micro-organismes, Université Henri Poincaré, Faculté des Sciences et Techniques, BP 239 54506 Vandoeuvre Cedex, France. gelhaye@lcb.uhp-nancy.fr</Affiliation>
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<Initials>DB</Initials>
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<ForeName>Pierre</ForeName>
<Initials>P</Initials>
</Author>
<Author ValidYN="Y"><LastName>Meyer</LastName>
<ForeName>Yves</ForeName>
<Initials>Y</Initials>
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<Author ValidYN="Y"><LastName>Jacquot</LastName>
<ForeName>Jean-Pierre</ForeName>
<Initials>JP</Initials>
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<Language>eng</Language>
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<MeshHeading><DescriptorName UI="D054480" MajorTopicYN="N">Thioredoxin h</DescriptorName>
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A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase.

A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase.

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