PoplarRustV1, Main, Exploration, bibRecord, 000094

Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.

Identifieur interne : 000094 ( Main/Exploration ); précédent : 000093; suivant : 000095

Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.

Auteurs : Nicolas Rouhier ; Eric Gelhaye ; Jose M. Gualberto ; Marie-Noelle Jordy ; Elisabeth De Fay ; Masakazu Hirasawa ; Sebastien Duplessis ; Stephane D. Lemaire ; Pascal Frey ; Francis Martin ; Wanda Manieri ; David B. Knaff ; Jean-Pierre Jacquot

Source :

Plant physiology [ 0032-0889 ] ; 2004.

RBID : pubmed:14976238

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Antioxidants (metabolism), Base Sequence (MeSH), Catalytic Domain (genetics), Chloroplast Thioredoxins (MeSH), Chloroplasts (metabolism), DNA, Plant (genetics), Dimerization (MeSH), Electron Transport (MeSH), Gene Expression (MeSH), Genes, Plant (MeSH), Macromolecular Substances (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Peroxiredoxins (MeSH), Plant Diseases (genetics), Plant Diseases (microbiology), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (genetics), Populus (metabolism), Populus (microbiology), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), Thioredoxins (metabolism).
MESH :
- chemical , chemistry : Peroxidases, Plant Proteins, Recombinant Proteins.
- chemical , genetics : DNA, Plant, Peroxidases, Plant Proteins, Recombinant Proteins.
- chemical , metabolism : Antioxidants, Peroxidases, Plant Proteins, Recombinant Proteins, Thioredoxins.
- genetics : Catalytic Domain, Plant Diseases, Populus.
- metabolism : Chloroplasts, Populus.
- microbiology : Plant Diseases, Populus.
- Amino Acid Sequence, Base Sequence, Chloroplast Thioredoxins, Dimerization, Electron Transport, Gene Expression, Genes, Plant, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Site-Directed, Oxidation-Reduction, Peroxiredoxins, Sequence Homology, Amino Acid, Substrate Specificity.

Abstract

Peroxiredoxins are ubiquitous thioredoxin- or glutaredoxin-dependent peroxidases, the function of which is to destroy peroxides. Peroxiredoxin Q, one of the four plant subtypes, is a homolog of the bacterial bacterioferritin comigratory proteins. We show here that the poplar (Populus tremula x Populus tremuloides) protein acts as a monomer with an intramolecular disulfide bridge between two conserved cysteines. A wide range of electron donors and substrates was tested. Unlike type II peroxiredoxin, peroxiredoxin Q cannot use the glutaredoxin or cyclophilin isoforms tested, but various cytosolic, chloroplastic, and mitochondrial thioredoxins are efficient electron donors with no marked specificities. The redox midpoint potential of the peroxiredoxin Q catalytic disulfide is -325 mV at pH 7.0, explaining why the wild-type protein is reduced by thioredoxin but not by glutaredoxin. Additional evidence that thioredoxin serves as a donor comes from the formation of heterodimers between peroxiredoxin Q and monocysteinic mutants of spinach (Spinacia oleracea) thioredoxin m. Peroxiredoxin Q can reduce various alkyl hydroperoxides, but with a better efficiency for cumene hydroperoxide than hydrogen peroxide and tertiary butyl hydroperoxide. The use of immunolocalization and of a green fluorescence protein fusion construct indicates that the transit sequence efficiently targets peroxiredoxin Q to the chloroplasts and especially to those of the guard cells. The expression of this protein and of type II peroxiredoxin is modified in response to an infection by two races of Melampsora larici-populina, the causative agent of the poplar rust. In the case of an hypersensitive response, the peroxiredoxin expression increased, whereas it decreased during a compatible interaction.

DOI: 10.1104/pp.103.035865
PubMed: 14976238
PubMed Central: PMC389925

Affiliations:

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

to stream Main, to step Corpus: 000103
to stream Main, to step Curation: 000103

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Antioxidants (metabolism)</term>
<term>Base Sequence (MeSH)</term>
<term>Catalytic Domain (genetics)</term>
<term>Chloroplast Thioredoxins (MeSH)</term>
<term>Chloroplasts (metabolism)</term>
<term>DNA, Plant (genetics)</term>
<term>Dimerization (MeSH)</term>
<term>Electron Transport (MeSH)</term>
<term>Gene Expression (MeSH)</term>
<term>Genes, Plant (MeSH)</term>
<term>Macromolecular Substances (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (genetics)</term>
<term>Peroxidases (metabolism)</term>
<term>Peroxiredoxins (MeSH)</term>
<term>Plant Diseases (genetics)</term>
<term>Plant Diseases (microbiology)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Populus (genetics)</term>
<term>Populus (metabolism)</term>
<term>Populus (microbiology)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Thioredoxins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN des plantes (génétique)</term>
<term>Antioxydants (métabolisme)</term>
<term>Chloroplastes (métabolisme)</term>
<term>Dimérisation (MeSH)</term>
<term>Domaine catalytique (génétique)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Expression des gènes (MeSH)</term>
<term>Gènes de plante (MeSH)</term>
<term>Maladies des plantes (génétique)</term>
<term>Maladies des plantes (microbiologie)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxidases (composition chimique)</term>
<term>Peroxidases (génétique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Peroxirédoxines (MeSH)</term>
<term>Populus (génétique)</term>
<term>Populus (microbiologie)</term>
<term>Populus (métabolisme)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Structures macromoléculaires (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Thiorédoxines (métabolisme)</term>
<term>Thiorédoxines chloroplastiques (MeSH)</term>
<term>Transport d'électrons (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Plant</term>
<term>Peroxidases</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term>
<term>Peroxidases</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Catalytic Domain</term>
<term>Plant Diseases</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN des plantes</term>
<term>Domaine catalytique</term>
<term>Maladies des plantes</term>
<term>Peroxidases</term>
<term>Populus</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chloroplasts</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Maladies des plantes</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Plant Diseases</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term>
<term>Chloroplastes</term>
<term>Peroxidases</term>
<term>Populus</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Chloroplast Thioredoxins</term>
<term>Dimerization</term>
<term>Electron Transport</term>
<term>Gene Expression</term>
<term>Genes, Plant</term>
<term>Macromolecular Substances</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Oxidation-Reduction</term>
<term>Peroxiredoxins</term>
<term>Sequence Homology, Amino Acid</term>
<term>Substrate Specificity</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Dimérisation</term>
<term>Données de séquences moléculaires</term>
<term>Expression des gènes</term>
<term>Gènes de plante</term>
<term>Mutagenèse dirigée</term>
<term>Oxydoréduction</term>
<term>Peroxirédoxines</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Spécificité du substrat</term>
<term>Structures macromoléculaires</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Thiorédoxines chloroplastiques</term>
<term>Transport d'électrons</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Peroxiredoxins are ubiquitous thioredoxin- or glutaredoxin-dependent peroxidases, the function of which is to destroy peroxides. Peroxiredoxin Q, one of the four plant subtypes, is a homolog of the bacterial bacterioferritin comigratory proteins. We show here that the poplar (Populus tremula x Populus tremuloides) protein acts as a monomer with an intramolecular disulfide bridge between two conserved cysteines. A wide range of electron donors and substrates was tested. Unlike type II peroxiredoxin, peroxiredoxin Q cannot use the glutaredoxin or cyclophilin isoforms tested, but various cytosolic, chloroplastic, and mitochondrial thioredoxins are efficient electron donors with no marked specificities. The redox midpoint potential of the peroxiredoxin Q catalytic disulfide is -325 mV at pH 7.0, explaining why the wild-type protein is reduced by thioredoxin but not by glutaredoxin. Additional evidence that thioredoxin serves as a donor comes from the formation of heterodimers between peroxiredoxin Q and monocysteinic mutants of spinach (Spinacia oleracea) thioredoxin m. Peroxiredoxin Q can reduce various alkyl hydroperoxides, but with a better efficiency for cumene hydroperoxide than hydrogen peroxide and tertiary butyl hydroperoxide. The use of immunolocalization and of a green fluorescence protein fusion construct indicates that the transit sequence efficiently targets peroxiredoxin Q to the chloroplasts and especially to those of the guard cells. The expression of this protein and of type II peroxiredoxin is modified in response to an infection by two races of Melampsora larici-populina, the causative agent of the poplar rust. In the case of an hypersensitive response, the peroxiredoxin expression increased, whereas it decreased during a compatible interaction.</div>
</front>
</TEI>
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<DateCompleted><Year>2004</Year>
<Month>05</Month>
<Day>27</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
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<JournalIssue CitedMedium="Print"><Volume>134</Volume>
<Issue>3</Issue>
<PubDate><Year>2004</Year>
<Month>Mar</Month>
</PubDate>
</JournalIssue>
<Title>Plant physiology</Title>
<ISOAbbreviation>Plant Physiol</ISOAbbreviation>
</Journal>
<ArticleTitle>Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.</ArticleTitle>
<Pagination><MedlinePgn>1027-38</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Peroxiredoxins are ubiquitous thioredoxin- or glutaredoxin-dependent peroxidases, the function of which is to destroy peroxides. Peroxiredoxin Q, one of the four plant subtypes, is a homolog of the bacterial bacterioferritin comigratory proteins. We show here that the poplar (Populus tremula x Populus tremuloides) protein acts as a monomer with an intramolecular disulfide bridge between two conserved cysteines. A wide range of electron donors and substrates was tested. Unlike type II peroxiredoxin, peroxiredoxin Q cannot use the glutaredoxin or cyclophilin isoforms tested, but various cytosolic, chloroplastic, and mitochondrial thioredoxins are efficient electron donors with no marked specificities. The redox midpoint potential of the peroxiredoxin Q catalytic disulfide is -325 mV at pH 7.0, explaining why the wild-type protein is reduced by thioredoxin but not by glutaredoxin. Additional evidence that thioredoxin serves as a donor comes from the formation of heterodimers between peroxiredoxin Q and monocysteinic mutants of spinach (Spinacia oleracea) thioredoxin m. Peroxiredoxin Q can reduce various alkyl hydroperoxides, but with a better efficiency for cumene hydroperoxide than hydrogen peroxide and tertiary butyl hydroperoxide. The use of immunolocalization and of a green fluorescence protein fusion construct indicates that the transit sequence efficiently targets peroxiredoxin Q to the chloroplasts and especially to those of the guard cells. The expression of this protein and of type II peroxiredoxin is modified in response to an infection by two races of Melampsora larici-populina, the causative agent of the poplar rust. In the case of an hypersensitive response, the peroxiredoxin expression increased, whereas it decreased during a compatible interaction.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Unité Mixte de Recherche Institut National de la Recherche Agronomique-Université Henri Poincaré 1136, Interactions Arbres/Micro-Organismes, Université Henri Poincaré, Faculté des Sciences, BP 239, 54506 Vandoeuvre cedex France.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Gelhaye</LastName>
<ForeName>Eric</ForeName>
<Initials>E</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gualberto</LastName>
<ForeName>Jose M</ForeName>
<Initials>JM</Initials>
</Author>
<Author ValidYN="Y"><LastName>Jordy</LastName>
<ForeName>Marie-Noelle</ForeName>
<Initials>MN</Initials>
</Author>
<Author ValidYN="Y"><LastName>De Fay</LastName>
<ForeName>Elisabeth</ForeName>
<Initials>E</Initials>
</Author>
<Author ValidYN="Y"><LastName>Hirasawa</LastName>
<ForeName>Masakazu</ForeName>
<Initials>M</Initials>
</Author>
<Author ValidYN="Y"><LastName>Duplessis</LastName>
<ForeName>Sebastien</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lemaire</LastName>
<ForeName>Stephane D</ForeName>
<Initials>SD</Initials>
</Author>
<Author ValidYN="Y"><LastName>Frey</LastName>
<ForeName>Pascal</ForeName>
<Initials>P</Initials>
</Author>
<Author ValidYN="Y"><LastName>Martin</LastName>
<ForeName>Francis</ForeName>
<Initials>F</Initials>
</Author>
<Author ValidYN="Y"><LastName>Manieri</LastName>
<ForeName>Wanda</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Knaff</LastName>
<ForeName>David B</ForeName>
<Initials>DB</Initials>
</Author>
<Author ValidYN="Y"><LastName>Jacquot</LastName>
<ForeName>Jean-Pierre</ForeName>
<Initials>JP</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2004</Year>
<Month>02</Month>
<Day>19</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Plant Physiol</MedlineTA>
<NlmUniqueID>0401224</NlmUniqueID>
<ISSNLinking>0032-0889</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054479">Chloroplast Thioredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D018744">DNA, Plant</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D046911">Macromolecular Substances</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>52500-60-4</RegistryNumber>
<NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
<NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber>
<NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance>
</Chemical>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName>
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Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.

Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.

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