Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.
Identifieur interne : 003D50 ( Main/Exploration ); précédent : 003D49; suivant : 003D51Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.
Auteurs : Nicolas Navrot [France] ; Valérie Collin ; José Gualberto ; Eric Gelhaye ; Masakazu Hirasawa ; Pascal Rey ; David B. Knaff ; Emmanuelle Issakidis ; Jean-Pierre Jacquot ; Nicolas RouhierSource :
- Plant physiology [ 0032-0889 ] ; 2006.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Données de séquences moléculaires (MeSH), Glutathione peroxidase (analyse), Glutathione peroxidase (composition chimique), Glutathione peroxidase (physiologie), Génome végétal (MeSH), Isoformes de protéines (analyse), Isoformes de protéines (composition chimique), Isoformes de protéines (physiologie), Oxydoréduction (MeSH), Peroxydes (métabolisme), Phylogenèse (MeSH), Populus (composition chimique), Populus (enzymologie), Populus (génétique), Protéines de fusion recombinantes (analyse), Protéines végétales (analyse), Protéines végétales (composition chimique), Protéines végétales (physiologie), Protéines à fluorescence verte (analyse), Régulation de l'expression des gènes végétaux (MeSH), Sites de fixation (MeSH), Spécificité du substrat (MeSH), Stress oxydatif (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (métabolisme).
- MESH :
- analyse : Glutathione peroxidase, Isoformes de protéines, Protéines de fusion recombinantes, Protéines végétales, Protéines à fluorescence verte.
- composition chimique : Glutathione peroxidase, Isoformes de protéines, Populus, Protéines végétales.
- enzymologie : Populus.
- génétique : Populus.
- métabolisme : Peroxydes, Thiorédoxines.
- physiologie : Glutathione peroxidase, Isoformes de protéines, Protéines végétales.
- Alignement de séquences, Données de séquences moléculaires, Génome végétal, Oxydoréduction, Phylogenèse, Régulation de l'expression des gènes végétaux, Sites de fixation, Spécificité du substrat, Stress oxydatif, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Gene Expression Regulation, Plant (MeSH), Genome, Plant (MeSH), Glutathione Peroxidase (analysis), Glutathione Peroxidase (chemistry), Glutathione Peroxidase (physiology), Green Fluorescent Proteins (analysis), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Peroxides (metabolism), Phylogeny (MeSH), Plant Proteins (analysis), Plant Proteins (chemistry), Plant Proteins (physiology), Populus (chemistry), Populus (enzymology), Populus (genetics), Protein Isoforms (analysis), Protein Isoforms (chemistry), Protein Isoforms (physiology), Recombinant Fusion Proteins (analysis), Sequence Alignment (MeSH), Substrate Specificity (MeSH), Thioredoxins (metabolism).
- MESH :
- chemical , analysis : Glutathione Peroxidase, Green Fluorescent Proteins, Plant Proteins, Protein Isoforms, Recombinant Fusion Proteins.
- chemical , chemistry : Glutathione Peroxidase, Plant Proteins, Protein Isoforms.
- chemical , metabolism : Peroxides, Thioredoxins.
- chemical , physiology : Glutathione Peroxidase, Plant Proteins, Protein Isoforms.
- chemistry : Populus.
- enzymology : Populus.
- genetics : Populus.
- Amino Acid Sequence, Binding Sites, Gene Expression Regulation, Plant, Genome, Plant, Molecular Sequence Data, Oxidation-Reduction, Oxidative Stress, Phylogeny, Sequence Alignment, Substrate Specificity.
Abstract
We provide here an exhaustive overview of the glutathione (GSH) peroxidase (Gpx) family of poplar (Populus trichocarpa). Although these proteins were initially defined as GSH dependent, in fact they use only reduced thioredoxin (Trx) for their regeneration and do not react with GSH or glutaredoxin, constituting a fifth class of peroxiredoxins. The two chloroplastic Gpxs display a marked selectivity toward their electron donors, being exclusively specific for Trxs of the y type for their reduction. In contrast, poplar Gpxs are much less specific with regard to their electron-accepting substrates, reducing hydrogen peroxide and more complex hydroperoxides equally well. Site-directed mutagenesis indicates that the catalytic mechanism and the Trx-mediated recycling process involve only two (cysteine [Cys]-107 and Cys-155) of the three conserved Cys, which form a disulfide bridge with an oxidation-redox midpoint potential of -295 mV. The reduction/formation of this disulfide is detected both by a shift on sodium dodecyl sulfate-polyacrylamide gel electrophoresis or by measuring the intrinsic tryptophan fluorescence of the protein. The six genes identified coding for Gpxs are expressed in various poplar organs, and two of them are localized in the chloroplast, with one colocalizing in mitochondria, suggesting a broad distribution of Gpxs in plant cells. The abundance of some Gpxs is modified in plants subjected to environmental constraints, generally increasing during fungal infection, water deficit, and metal stress, and decreasing during photooxidative stress, showing that Gpx proteins are involved in the response to both biotic and abiotic stress conditions.
DOI: 10.1104/pp.106.089458
PubMed: 17071643
PubMed Central: PMC1676047
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.</title><author><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name><affiliation wicri:level="3"><nlm:affiliation>Unité Mixte de Recherche Institut National de la Recherche Agronomique-Université Henri Poincaré 1136, Université Henri Poincaré, 54506 Vandoeuvre cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité Mixte de Recherche Institut National de la Recherche Agronomique-Université Henri Poincaré 1136, Université Henri Poincaré, 54506 Vandoeuvre cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandoeuvre</settlement></placeName></affiliation></author><author><name sortKey="Collin, Valerie" sort="Collin, Valerie" uniqKey="Collin V" first="Valérie" last="Collin">Valérie Collin</name></author><author><name sortKey="Gualberto, Jose" sort="Gualberto, Jose" uniqKey="Gualberto J" first="José" last="Gualberto">José Gualberto</name></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author><author><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name></author><author><name sortKey="Rey, Pascal" sort="Rey, Pascal" uniqKey="Rey P" first="Pascal" last="Rey">Pascal Rey</name></author><author><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name></author><author><name sortKey="Issakidis, Emmanuelle" sort="Issakidis, Emmanuelle" uniqKey="Issakidis E" first="Emmanuelle" last="Issakidis">Emmanuelle Issakidis</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:17071643</idno><idno type="pmid">17071643</idno><idno type="doi">10.1104/pp.106.089458</idno><idno type="pmc">PMC1676047</idno><idno type="wicri:Area/Main/Corpus">003D01</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003D01</idno><idno type="wicri:Area/Main/Curation">003D01</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003D01</idno><idno type="wicri:Area/Main/Exploration">003D01</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.</title><author><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name><affiliation wicri:level="3"><nlm:affiliation>Unité Mixte de Recherche Institut National de la Recherche Agronomique-Université Henri Poincaré 1136, Université Henri Poincaré, 54506 Vandoeuvre cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité Mixte de Recherche Institut National de la Recherche Agronomique-Université Henri Poincaré 1136, Université Henri Poincaré, 54506 Vandoeuvre cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandoeuvre</settlement></placeName></affiliation></author><author><name sortKey="Collin, Valerie" sort="Collin, Valerie" uniqKey="Collin V" first="Valérie" last="Collin">Valérie Collin</name></author><author><name sortKey="Gualberto, Jose" sort="Gualberto, Jose" uniqKey="Gualberto J" first="José" last="Gualberto">José Gualberto</name></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author><author><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name></author><author><name sortKey="Rey, Pascal" sort="Rey, Pascal" uniqKey="Rey P" first="Pascal" last="Rey">Pascal Rey</name></author><author><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name></author><author><name sortKey="Issakidis, Emmanuelle" sort="Issakidis, Emmanuelle" uniqKey="Issakidis E" first="Emmanuelle" last="Issakidis">Emmanuelle Issakidis</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author></analytic><series><title level="j">Plant physiology</title><idno type="ISSN">0032-0889</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Genome, Plant (MeSH)</term><term>Glutathione Peroxidase (analysis)</term><term>Glutathione Peroxidase (chemistry)</term><term>Glutathione Peroxidase (physiology)</term><term>Green Fluorescent Proteins (analysis)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Peroxides (metabolism)</term><term>Phylogeny (MeSH)</term><term>Plant Proteins (analysis)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (physiology)</term><term>Populus (chemistry)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Protein Isoforms (analysis)</term><term>Protein Isoforms (chemistry)</term><term>Protein Isoforms (physiology)</term><term>Recombinant Fusion Proteins (analysis)</term><term>Sequence Alignment (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutathione peroxidase (analyse)</term><term>Glutathione peroxidase (composition chimique)</term><term>Glutathione peroxidase (physiologie)</term><term>Génome végétal (MeSH)</term><term>Isoformes de protéines (analyse)</term><term>Isoformes de protéines (composition chimique)</term><term>Isoformes de protéines (physiologie)</term><term>Oxydoréduction (MeSH)</term><term>Peroxydes (métabolisme)</term><term>Phylogenèse (MeSH)</term><term>Populus (composition chimique)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Protéines de fusion recombinantes (analyse)</term><term>Protéines végétales (analyse)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (physiologie)</term><term>Protéines à fluorescence verte (analyse)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Glutathione Peroxidase</term><term>Green Fluorescent Proteins</term><term>Plant Proteins</term><term>Protein Isoforms</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Peroxidase</term><term>Plant Proteins</term><term>Protein Isoforms</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peroxides</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Glutathione Peroxidase</term><term>Plant Proteins</term><term>Protein Isoforms</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Glutathione peroxidase</term><term>Isoformes de protéines</term><term>Protéines de fusion recombinantes</term><term>Protéines végétales</term><term>Protéines à fluorescence verte</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathione peroxidase</term><term>Isoformes de protéines</term><term>Populus</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peroxydes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glutathione peroxidase</term><term>Isoformes de protéines</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Gene Expression Regulation, Plant</term><term>Genome, Plant</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Phylogeny</term><term>Sequence Alignment</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Données de séquences moléculaires</term><term>Génome végétal</term><term>Oxydoréduction</term><term>Phylogenèse</term><term>Régulation de l'expression des gènes végétaux</term><term>Sites de fixation</term><term>Spécificité du substrat</term><term>Stress oxydatif</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We provide here an exhaustive overview of the glutathione (GSH) peroxidase (Gpx) family of poplar (Populus trichocarpa). Although these proteins were initially defined as GSH dependent, in fact they use only reduced thioredoxin (Trx) for their regeneration and do not react with GSH or glutaredoxin, constituting a fifth class of peroxiredoxins. The two chloroplastic Gpxs display a marked selectivity toward their electron donors, being exclusively specific for Trxs of the y type for their reduction. In contrast, poplar Gpxs are much less specific with regard to their electron-accepting substrates, reducing hydrogen peroxide and more complex hydroperoxides equally well. Site-directed mutagenesis indicates that the catalytic mechanism and the Trx-mediated recycling process involve only two (cysteine [Cys]-107 and Cys-155) of the three conserved Cys, which form a disulfide bridge with an oxidation-redox midpoint potential of -295 mV. The reduction/formation of this disulfide is detected both by a shift on sodium dodecyl sulfate-polyacrylamide gel electrophoresis or by measuring the intrinsic tryptophan fluorescence of the protein. The six genes identified coding for Gpxs are expressed in various poplar organs, and two of them are localized in the chloroplast, with one colocalizing in mitochondria, suggesting a broad distribution of Gpxs in plant cells. The abundance of some Gpxs is modified in plants subjected to environmental constraints, generally increasing during fungal infection, water deficit, and metal stress, and decreasing during photooxidative stress, showing that Gpx proteins are involved in the response to both biotic and abiotic stress conditions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17071643</PMID><DateCompleted><Year>2007</Year><Month>03</Month><Day>20</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>142</Volume><Issue>4</Issue><PubDate><Year>2006</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.</ArticleTitle><Pagination><MedlinePgn>1364-79</MedlinePgn></Pagination><Abstract><AbstractText>We provide here an exhaustive overview of the glutathione (GSH) peroxidase (Gpx) family of poplar (Populus trichocarpa). Although these proteins were initially defined as GSH dependent, in fact they use only reduced thioredoxin (Trx) for their regeneration and do not react with GSH or glutaredoxin, constituting a fifth class of peroxiredoxins. The two chloroplastic Gpxs display a marked selectivity toward their electron donors, being exclusively specific for Trxs of the y type for their reduction. In contrast, poplar Gpxs are much less specific with regard to their electron-accepting substrates, reducing hydrogen peroxide and more complex hydroperoxides equally well. Site-directed mutagenesis indicates that the catalytic mechanism and the Trx-mediated recycling process involve only two (cysteine [Cys]-107 and Cys-155) of the three conserved Cys, which form a disulfide bridge with an oxidation-redox midpoint potential of -295 mV. The reduction/formation of this disulfide is detected both by a shift on sodium dodecyl sulfate-polyacrylamide gel electrophoresis or by measuring the intrinsic tryptophan fluorescence of the protein. The six genes identified coding for Gpxs are expressed in various poplar organs, and two of them are localized in the chloroplast, with one colocalizing in mitochondria, suggesting a broad distribution of Gpxs in plant cells. The abundance of some Gpxs is modified in plants subjected to environmental constraints, generally increasing during fungal infection, water deficit, and metal stress, and decreasing during photooxidative stress, showing that Gpx proteins are involved in the response to both biotic and abiotic stress conditions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Navrot</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherche Institut National de la Recherche Agronomique-Université Henri Poincaré 1136, Université Henri Poincaré, 54506 Vandoeuvre cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Collin</LastName><ForeName>Valérie</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Gualberto</LastName><ForeName>José</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Hirasawa</LastName><ForeName>Masakazu</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Rey</LastName><ForeName>Pascal</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Knaff</LastName><ForeName>David B</ForeName><Initials>DB</Initials></Author><Author ValidYN="Y"><LastName>Issakidis</LastName><ForeName>Emmanuelle</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</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>2006</Year><Month>10</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010545">Peroxides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018745" MajorTopicYN="N">Genome, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005979" MajorTopicYN="N">Glutathione Peroxidase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010545" MajorTopicYN="N">Peroxides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>10</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>3</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>10</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17071643</ArticleId><ArticleId IdType="pii">pp.106.089458</ArticleId><ArticleId IdType="doi">10.1104/pp.106.089458</ArticleId><ArticleId IdType="pmc">PMC1676047</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biol Chem. 2000 Nov 17;275(46):35908-13</Citation><ArticleIdList><ArticleId IdType="pubmed">10964927</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2005 Sep 6;44(35):11864-71</Citation><ArticleIdList><ArticleId IdType="pubmed">16128588</ArticleId></ArticleIdList></Reference><Reference><Citation>Planta. 2004 Sep;219(5):784-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15164287</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1997 Jan 6;400(3):293-6</Citation><ArticleIdList><ArticleId IdType="pubmed">9009217</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 2002 Nov 15;111(4):471-81</Citation><ArticleIdList><ArticleId IdType="pubmed">12437921</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Sep 15;275(37):28715-21</Citation><ArticleIdList><ArticleId IdType="pubmed">10874045</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2004 Dec;136(4):4088-95</Citation><ArticleIdList><ArticleId IdType="pubmed">15531707</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell Rep. 2006 Oct;25(10):1122-32</Citation><ArticleIdList><ArticleId IdType="pubmed">16807751</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2004 Mar;134(3):1027-38</Citation><ArticleIdList><ArticleId IdType="pubmed">14976238</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2000 Aug 22;39(33):10172-6</Citation><ArticleIdList><ArticleId IdType="pubmed">10956006</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant J. 2004 Jan;37(1):21-33</Citation><ArticleIdList><ArticleId IdType="pubmed">14675429</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Jun 27;278(26):23747-52</Citation><ArticleIdList><ArticleId IdType="pubmed">12707279</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2002 Jul 15;21(14):3681-93</Citation><ArticleIdList><ArticleId IdType="pubmed">12110581</ArticleId></ArticleIdList></Reference><Reference><Citation>Free Radic Biol Med. 2005 Jun 1;38(11):1413-21</Citation><ArticleIdList><ArticleId IdType="pubmed">15890615</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 2005 Dec;17(12):3451-69</Citation><ArticleIdList><ArticleId IdType="pubmed">16258032</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1998 Jul 1;255(1):185-95</Citation><ArticleIdList><ArticleId IdType="pubmed">9692918</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 May 26;275(21):16296-301</Citation><ArticleIdList><ArticleId IdType="pubmed">10821871</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Dec 23;280(51):42078-87</Citation><ArticleIdList><ArticleId IdType="pubmed">16251189</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2001 Nov;127(3):1299-309</Citation><ArticleIdList><ArticleId IdType="pubmed">11706208</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant J. 2003 Dec;36(5):602-15</Citation><ArticleIdList><ArticleId IdType="pubmed">14617062</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2004 Jul;135(3):1630-41</Citation><ArticleIdList><ArticleId IdType="pubmed">15235116</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1994 Jan 3;337(1):52-5</Citation><ArticleIdList><ArticleId IdType="pubmed">8276113</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Mar 9;276(10):7397-403</Citation><ArticleIdList><ArticleId IdType="pubmed">11087748</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2000 Sep 7;1493(1-2):225-30</Citation><ArticleIdList><ArticleId IdType="pubmed">10978528</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2004 Sep;136(1):2621-32</Citation><ArticleIdList><ArticleId IdType="pubmed">15375207</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Oct 5;101(40):14545-50</Citation><ArticleIdList><ArticleId IdType="pubmed">15385674</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant J. 1998 Feb;13(3):375-9</Citation><ArticleIdList><ArticleId IdType="pubmed">9680987</ArticleId></ArticleIdList></Reference><Reference><Citation>Biotechniques. 1995 Aug;19(2):196-8, 200</Citation><ArticleIdList><ArticleId IdType="pubmed">8527135</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cells. 2004 Feb 29;17(1):23-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15055522</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 Jul 19;277(29):25983-91</Citation><ArticleIdList><ArticleId IdType="pubmed">11973339</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 2002 May;269(9):2414-20</Citation><ArticleIdList><ArticleId IdType="pubmed">11985625</ArticleId></ArticleIdList></Reference><Reference><Citation>Photosynth Res. 2002;74(3):259-68</Citation><ArticleIdList><ArticleId IdType="pubmed">16245137</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2003 Aug;132(4):2045-57</Citation><ArticleIdList><ArticleId IdType="pubmed">12913160</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Cell Biol. 2005 Apr;17(2):183-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15780595</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol Biochem. 2005 Feb;43(2):107-16</Citation><ArticleIdList><ArticleId IdType="pubmed">15820657</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Plant Physiol Plant Mol Biol. 1998 Jun;49:249-279</Citation><ArticleIdList><ArticleId IdType="pubmed">15012235</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1998 Apr 15;253(2):445-51</Citation><ArticleIdList><ArticleId IdType="pubmed">9654095</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Plant Biol. 2003 Aug;6(4):379-89</Citation><ArticleIdList><ArticleId IdType="pubmed">12873534</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Nov 21;278(47):46869-77</Citation><ArticleIdList><ArticleId IdType="pubmed">12954611</ArticleId></ArticleIdList></Reference><Reference><Citation>Planta. 2005 Sep;222(1):192-200</Citation><ArticleIdList><ArticleId IdType="pubmed">15843961</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):11014-9</Citation><ArticleIdList><ArticleId IdType="pubmed">9724821</ArticleId></ArticleIdList></Reference><Reference><Citation>J Exp Bot. 2006;57(8):1685-96</Citation><ArticleIdList><ArticleId IdType="pubmed">16720602</ArticleId></ArticleIdList></Reference><Reference><Citation>Gene. 2002 Jan 23;283(1-2):227-36</Citation><ArticleIdList><ArticleId IdType="pubmed">11867229</ArticleId></ArticleIdList></Reference><Reference><Citation>Biometals. 2007 Feb;20(1):27-36</Citation><ArticleIdList><ArticleId IdType="pubmed">16752220</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 Apr 12;277(15):12572-8</Citation><ArticleIdList><ArticleId IdType="pubmed">11823460</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2005 Jan 17;1703(2):231-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15680231</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2003 May 8;542(1-3):37-41</Citation><ArticleIdList><ArticleId IdType="pubmed">12729894</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Mol Biol. 1992 Feb;18(3):623-7</Citation><ArticleIdList><ArticleId IdType="pubmed">1536938</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1999 Oct 1;459(1):33-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10508912</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2005 Jun;138(2):909-22</Citation><ArticleIdList><ArticleId IdType="pubmed">15923321</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1990;186:448-57</Citation><ArticleIdList><ArticleId IdType="pubmed">2233312</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Nov 5;279(45):46652-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15337745</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8875-80</Citation><ArticleIdList><ArticleId IdType="pubmed">15956211</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2005 Feb 15;44(6):1755-67</Citation><ArticleIdList><ArticleId IdType="pubmed">15697201</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Apr 1;280(13):12168-80</Citation><ArticleIdList><ArticleId IdType="pubmed">15632145</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Genet Syst. 1997 Oct;72(5):311-6</Citation><ArticleIdList><ArticleId IdType="pubmed">9511228</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1999 Apr 20;38(16):5200-5</Citation><ArticleIdList><ArticleId IdType="pubmed">10213627</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Feb 10;281(6):3418-24</Citation><ArticleIdList><ArticleId IdType="pubmed">16354655</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Vandoeuvre</li></settlement></list><tree><noCountry><name sortKey="Collin, Valerie" sort="Collin, Valerie" uniqKey="Collin V" first="Valérie" last="Collin">Valérie Collin</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Gualberto, Jose" sort="Gualberto, Jose" uniqKey="Gualberto J" first="José" last="Gualberto">José Gualberto</name><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name><name sortKey="Issakidis, Emmanuelle" sort="Issakidis, Emmanuelle" uniqKey="Issakidis E" first="Emmanuelle" last="Issakidis">Emmanuelle Issakidis</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name><name sortKey="Rey, Pascal" sort="Rey, Pascal" uniqKey="Rey P" first="Pascal" last="Rey">Pascal Rey</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003D50 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003D50 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PoplarV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:17071643
|texte= Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:17071643" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |