Functional analysis and expression characteristics of chloroplastic Prx IIE.
Identifieur interne : 003919 ( Main/Exploration ); précédent : 003918; suivant : 003920Functional analysis and expression characteristics of chloroplastic Prx IIE.
Auteurs : Filipe Gama [France] ; Claire Bréhélin ; Eric Gelhaye ; Yves Meyer ; Jean-Pierre Jacquot ; Pascal Rey ; Nicolas RouhierSource :
- Physiologia plantarum [ 1399-3054 ] ; 2008.
Descripteurs français
- KwdFr :
- 2-Hydroperoxy-2-méthyl-propane (métabolisme), Arabidopsis (enzymologie), Arabidopsis (génétique), Arabidopsis (métabolisme), Chloroplastes (enzymologie), Chloroplastes (métabolisme), Données de séquences moléculaires (MeSH), Feuilles de plante (métabolisme), Glutarédoxines (métabolisme), Peroxirédoxines (génétique), Peroxirédoxines (métabolisme), Peroxyde d'hydrogène (métabolisme), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (métabolisme), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Technique de Western (MeSH), Thiorédoxines (métabolisme).
- MESH :
- enzymologie : Arabidopsis, Chloroplastes.
- génétique : Arabidopsis, Peroxirédoxines, Protéines d'Arabidopsis.
- métabolisme : 2-Hydroperoxy-2-méthyl-propane, Arabidopsis, Chloroplastes, Feuilles de plante, Glutarédoxines, Peroxirédoxines, Peroxyde d'hydrogène, Protéines d'Arabidopsis, Thiorédoxines.
- Données de séquences moléculaires, Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Technique de Western.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (enzymology), Arabidopsis (genetics), Arabidopsis (metabolism), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Blotting, Western (MeSH), Chloroplasts (enzymology), Chloroplasts (metabolism), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Glutaredoxins (metabolism), Hydrogen Peroxide (metabolism), Molecular Sequence Data (MeSH), Peroxiredoxins (genetics), Peroxiredoxins (metabolism), Plant Leaves (metabolism), Sequence Homology, Amino Acid (MeSH), Thioredoxins (metabolism), tert-Butylhydroperoxide (metabolism).
- MESH :
- chemical , genetics : Arabidopsis Proteins, Peroxiredoxins.
- enzymology : Arabidopsis, Chloroplasts.
- genetics : Arabidopsis.
- metabolism : Arabidopsis, Arabidopsis Proteins, Chloroplasts, Glutaredoxins, Hydrogen Peroxide, Peroxiredoxins, Plant Leaves, Thioredoxins, tert-Butylhydroperoxide.
- Amino Acid Sequence, Blotting, Western, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Molecular Sequence Data, Sequence Homology, Amino Acid.
Abstract
Peroxiredoxins (Prxs) are ubiquitous thiol-dependent peroxidases capable of eliminating a variety of peroxides through reactive catalytic cysteines, which are regenerated by reducing systems. Based on amino acid sequences and their mode of catalysis, five groups of thiol peroxidases have been distinguished in plants, and type II Prx is one of them with representatives in many sub-cellular compartments. The mature form of poplar chloroplastic Prx IIE was expressed as a recombinant protein in Escherichia coli. The protein is able to reduce H2O2 and tert-butyl hydroperoxide and is regenerated by both glutaredoxin (Grx) and thioredoxin (Trx) systems. Nevertheless, compared with Trxs, Grxs, and more especially chloroplastic Grx S12, are far more efficient reductants towards Prx IIE. The expression of Prx IIE at both the mRNA and protein levels as a function of organ type and abiotic stress conditions was investigated. Western blot analysis revealed that Prx IIE gene is constitutively expressed in Arabidopsis thaliana, mostly in young and mature leaves and in flowers. Under photo-oxidative treatment and water deficit, almost no change was observed in the abundance of Prx IIE in A. thaliana, while the level of Prx Q (one of the two other chloroplastic Prxs with 2-Cys Prx) increased in response to both stresses, indicating that plastidic members of the Prx family exhibit specific patterns of expression under stress.
DOI: 10.1111/j.1399-3054.2008.01097.x
PubMed: 18422870
Affiliations:
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Vandoeuvre-lès-Nancy Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité Mixte de Recherches 1136 INRA UHP (Interactions Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Université Henri Poincaré BP 239, 54506 Vandoeuvre-lès-Nancy Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandœuvre-lès-Nancy</settlement></placeName></affiliation></author><author><name sortKey="Brehelin, Claire" sort="Brehelin, Claire" uniqKey="Brehelin C" first="Claire" last="Bréhélin">Claire Bréhélin</name></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author><author><name sortKey="Meyer, Yves" sort="Meyer, Yves" uniqKey="Meyer Y" first="Yves" last="Meyer">Yves Meyer</name></author><author><name sortKey="Jacquot, Jean Pierre" 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(metabolism)</term><term>Gene Expression Regulation, Enzymologic (MeSH)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Glutaredoxins (metabolism)</term><term>Hydrogen Peroxide (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxiredoxins (genetics)</term><term>Peroxiredoxins (metabolism)</term><term>Plant Leaves (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Thioredoxins (metabolism)</term><term>tert-Butylhydroperoxide (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>2-Hydroperoxy-2-méthyl-propane (métabolisme)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (génétique)</term><term>Arabidopsis (métabolisme)</term><term>Chloroplastes (enzymologie)</term><term>Chloroplastes (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Feuilles de plante (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Peroxirédoxines 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Regulation, Enzymologic</term><term>Gene Expression Regulation, Plant</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Régulation de l'expression des gènes végétaux</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Technique de Western</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Peroxiredoxins (Prxs) are ubiquitous thiol-dependent peroxidases capable of eliminating a variety of peroxides through reactive catalytic cysteines, which are regenerated by reducing systems. Based on amino acid sequences and their mode of catalysis, five groups of thiol peroxidases have been distinguished in plants, and type II Prx is one of them with representatives in many sub-cellular compartments. The mature form of poplar chloroplastic Prx IIE was expressed as a recombinant protein in Escherichia coli. The protein is able to reduce H2O2 and tert-butyl hydroperoxide and is regenerated by both glutaredoxin (Grx) and thioredoxin (Trx) systems. Nevertheless, compared with Trxs, Grxs, and more especially chloroplastic Grx S12, are far more efficient reductants towards Prx IIE. The expression of Prx IIE at both the mRNA and protein levels as a function of organ type and abiotic stress conditions was investigated. Western blot analysis revealed that Prx IIE gene is constitutively expressed in Arabidopsis thaliana, mostly in young and mature leaves and in flowers. Under photo-oxidative treatment and water deficit, almost no change was observed in the abundance of Prx IIE in A. thaliana, while the level of Prx Q (one of the two other chloroplastic Prxs with 2-Cys Prx) increased in response to both stresses, indicating that plastidic members of the Prx family exhibit specific patterns of expression under stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18422870</PMID><DateCompleted><Year>2008</Year><Month>11</Month><Day>04</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-3054</ISSN><JournalIssue CitedMedium="Internet"><Volume>133</Volume><Issue>3</Issue><PubDate><Year>2008</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Physiologia plantarum</Title><ISOAbbreviation>Physiol Plant</ISOAbbreviation></Journal><ArticleTitle>Functional analysis and expression characteristics of chloroplastic Prx IIE.</ArticleTitle><Pagination><MedlinePgn>599-610</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1399-3054.2008.01097.x</ELocationID><Abstract><AbstractText>Peroxiredoxins (Prxs) are ubiquitous thiol-dependent peroxidases capable of eliminating a variety of peroxides through reactive catalytic cysteines, which are regenerated by reducing systems. Based on amino acid sequences and their mode of catalysis, five groups of thiol peroxidases have been distinguished in plants, and type II Prx is one of them with representatives in many sub-cellular compartments. The mature form of poplar chloroplastic Prx IIE was expressed as a recombinant protein in Escherichia coli. The protein is able to reduce H2O2 and tert-butyl hydroperoxide and is regenerated by both glutaredoxin (Grx) and thioredoxin (Trx) systems. Nevertheless, compared with Trxs, Grxs, and more especially chloroplastic Grx S12, are far more efficient reductants towards Prx IIE. The expression of Prx IIE at both the mRNA and protein levels as a function of organ type and abiotic stress conditions was investigated. Western blot analysis revealed that Prx IIE gene is constitutively expressed in Arabidopsis thaliana, mostly in young and mature leaves and in flowers. Under photo-oxidative treatment and water deficit, almost no change was observed in the abundance of Prx IIE in A. thaliana, while the level of Prx Q (one of the two other chloroplastic Prxs with 2-Cys Prx) increased in response to both stresses, indicating that plastidic members of the Prx family exhibit specific patterns of expression under stress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gama</LastName><ForeName>Filipe</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherches 1136 INRA UHP (Interactions Arbres Microorganismes), IFR 110 Génomique Ecophysiologie et Ecologie Fonctionnelles, Université Henri Poincaré BP 239, 54506 Vandoeuvre-lès-Nancy Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bréhélin</LastName><ForeName>Claire</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Meyer</LastName><ForeName>Yves</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Rey</LastName><ForeName>Pascal</ForeName><Initials>P</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>2008</Year><Month>07</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>Physiol Plant</MedlineTA><NlmUniqueID>1256322</NlmUniqueID><ISSNLinking>0031-9317</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>955VYL842B</RegistryNumber><NameOfSubstance UI="D020122">tert-Butylhydroperoxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002736" MajorTopicYN="N">Chloroplasts</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018515" MajorTopicYN="N">Plant Leaves</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020122" MajorTopicYN="N">tert-Butylhydroperoxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>4</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Meyer, Yves" sort="Meyer, Yves" uniqKey="Meyer Y" first="Yves" last="Meyer">Yves Meyer</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="Gama, Filipe" sort="Gama, Filipe" uniqKey="Gama F" first="Filipe" last="Gama">Filipe Gama</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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