Plastidic P2 glucose-6P dehydrogenase from poplar is modulated by thioredoxin m-type: Distinct roles of cysteine residues in redox regulation and NADPH inhibition.
Identifieur interne : 001719 ( Main/Exploration ); précédent : 001718; suivant : 001720Plastidic P2 glucose-6P dehydrogenase from poplar is modulated by thioredoxin m-type: Distinct roles of cysteine residues in redox regulation and NADPH inhibition.
Auteurs : Manuela Cardi [Italie] ; Mirko Zaffagnini [Italie] ; Alessia De Lillo [Italie] ; Daniela Castiglia [Italie] ; Kamel Chibani [France] ; José Manuel Gualberto [France] ; Nicolas Rouhier [France] ; Jean-Pierre Jacquot [France] ; Sergio Esposito [Italie]Source :
- Plant science : an international journal of experimental plant biology [ 1873-2259 ] ; 2016.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Clonage moléculaire (MeSH), Cystéine (composition chimique), Cystéine (physiologie), Glucose 6-phosphate dehydrogenase (composition chimique), Glucose 6-phosphate dehydrogenase (métabolisme), Glucose 6-phosphate dehydrogenase (physiologie), Motifs d'acides aminés (MeSH), Mutagenèse dirigée (MeSH), NADP (antagonistes et inhibiteurs), NADP (composition chimique), Oxydoréduction (MeSH), Plastes (métabolisme), Populus (génétique), Populus (métabolisme), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (métabolisme), Protéines végétales (physiologie), Sites de fixation (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme), Thiorédoxines (physiologie), Voie des pentoses phosphates (MeSH).
- MESH :
- antagonistes et inhibiteurs : NADP.
- composition chimique : Cystéine, Glucose 6-phosphate dehydrogenase, NADP, Protéines végétales, Thiorédoxines.
- génétique : Populus.
- métabolisme : Glucose 6-phosphate dehydrogenase, Plastes, Populus, Protéines recombinantes, Protéines végétales, Thiorédoxines.
- physiologie : Cystéine, Glucose 6-phosphate dehydrogenase, Protéines végétales, Thiorédoxines.
- Alignement de séquences, Clonage moléculaire, Motifs d'acides aminés, Mutagenèse dirigée, Oxydoréduction, Sites de fixation, Séquence d'acides aminés, Voie des pentoses phosphates.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Binding Sites (MeSH), Cloning, Molecular (MeSH), Cysteine (chemistry), Cysteine (physiology), Glucosephosphate Dehydrogenase (chemistry), Glucosephosphate Dehydrogenase (metabolism), Glucosephosphate Dehydrogenase (physiology), Mutagenesis, Site-Directed (MeSH), NADP (antagonists & inhibitors), NADP (chemistry), Oxidation-Reduction (MeSH), Pentose Phosphate Pathway (MeSH), Plant Proteins (chemistry), Plant Proteins (metabolism), Plant Proteins (physiology), Plastids (metabolism), Populus (genetics), Populus (metabolism), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Thioredoxins (chemistry), Thioredoxins (metabolism), Thioredoxins (physiology).
- MESH :
- chemical , antagonists & inhibitors : NADP.
- chemical , chemistry : Cysteine, Glucosephosphate Dehydrogenase, NADP, Plant Proteins, Thioredoxins.
- chemical , metabolism : Glucosephosphate Dehydrogenase, Plant Proteins, Recombinant Proteins, Thioredoxins.
- chemical , physiology : Cysteine, Glucosephosphate Dehydrogenase, Plant Proteins, Thioredoxins.
- genetics : Populus.
- metabolism : Plastids, Populus.
- Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Cloning, Molecular, Mutagenesis, Site-Directed, Oxidation-Reduction, Pentose Phosphate Pathway, Sequence Alignment.
Abstract
A cDNA coding for a plastidic P2-type G6PDH isoform from poplar (Populus tremula x tremuloides) has been used to express and purify to homogeneity the mature recombinant protein with a N-terminus His-tag. The study of the kinetic properties of the recombinant enzyme showed an in vitro redox sensing modulation exerted by reduced DTT. The interaction with thioredoxins (TRXs) was then investigated. Five cysteine to serine variants (C145S - C175S - C183S - C195S - C242S) and a variant with a double substitution for Cys175 and Cys183 (C175S/C183S) have been generated, purified and biochemically characterized in order to investigate the specific role(s) of cysteines in terms of redox regulation and NADPH-dependent inhibition. Three cysteine residues (C145, C194, C242) are suggested to have a role in controlling the NADP+ access to the active site, and in stabilizing the NADPH regulatory binding site. Our results also indicate that the regulatory disulfide involves residues Cys175 and Cys183 in a position similar to those of chloroplastic P1-G6PDHs, but the modulation is exerted primarily by TRX m-type, in contrast to P1-G6PDH, which is regulated by TRX f. This unexpected specificity indicates differences in the mechanism of regulation, and redox sensing of plastidic P2-G6PDH compared to chloroplastic P1-G6PDH in higher plants.
DOI: 10.1016/j.plantsci.2016.08.003
PubMed: 27717462
Affiliations:
- France, Italie
- Alsace (région administrative), Grand Est, Lorraine (région)
- Champenoux, Strasbourg
- Université de Lorraine, Université de Strasbourg
Links toward previous steps (curation, corpus...)
Le document en format XML
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INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Gualberto, Jose Manuel" sort="Gualberto, Jose Manuel" uniqKey="Gualberto J" first="José Manuel" last="Gualberto">José Manuel Gualberto</name><affiliation wicri:level="4"><nlm:affiliation>Université de Strasbourg, Institut de Biologie Moléculaire Des Plantes (IBMP), CNRS-UPR 2357, 67084 Strasbourg, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Strasbourg, Institut de Biologie Moléculaire Des Plantes (IBMP), CNRS-UPR 2357, 67084 Strasbourg</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Alsace (région administrative)</region><settlement type="city">Strasbourg</settlement></placeName><orgName type="university">Université de Strasbourg</orgName></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Esposito, Sergio" sort="Esposito, Sergio" uniqKey="Esposito S" first="Sergio" last="Esposito">Sergio Esposito</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy. Electronic address: sergio.esposito@unina.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli</wicri:regionArea><wicri:noRegion>I-80126 Napoli</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27717462</idno><idno type="pmid">27717462</idno><idno type="doi">10.1016/j.plantsci.2016.08.003</idno><idno type="wicri:Area/Main/Corpus">001605</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001605</idno><idno type="wicri:Area/Main/Curation">001605</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001605</idno><idno type="wicri:Area/Main/Exploration">001605</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Plastidic P2 glucose-6P dehydrogenase from poplar is modulated by thioredoxin m-type: Distinct roles of cysteine residues in redox regulation and NADPH inhibition.</title><author><name sortKey="Cardi, Manuela" sort="Cardi, Manuela" uniqKey="Cardi M" first="Manuela" last="Cardi">Manuela Cardi</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli</wicri:regionArea><wicri:noRegion>I-80126 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Zaffagnini, Mirko" sort="Zaffagnini, Mirko" uniqKey="Zaffagnini M" first="Mirko" last="Zaffagnini">Mirko Zaffagnini</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Farmacia e Biotecnologie, Univ. di Bologna, I-40126 Bologna, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Farmacia e Biotecnologie, Univ. di Bologna, I-40126 Bologna</wicri:regionArea><wicri:noRegion>I-40126 Bologna</wicri:noRegion></affiliation></author><author><name sortKey="De Lillo, Alessia" sort="De Lillo, Alessia" uniqKey="De Lillo A" first="Alessia" last="De Lillo">Alessia De Lillo</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli</wicri:regionArea><wicri:noRegion>I-80126 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Castiglia, Daniela" sort="Castiglia, Daniela" uniqKey="Castiglia D" first="Daniela" last="Castiglia">Daniela Castiglia</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli</wicri:regionArea><wicri:noRegion>I-80126 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Chibani, Kamel" sort="Chibani, Kamel" uniqKey="Chibani K" first="Kamel" last="Chibani">Kamel Chibani</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Gualberto, Jose Manuel" sort="Gualberto, Jose Manuel" uniqKey="Gualberto J" first="José Manuel" last="Gualberto">José Manuel Gualberto</name><affiliation wicri:level="4"><nlm:affiliation>Université de Strasbourg, Institut de Biologie Moléculaire Des Plantes (IBMP), CNRS-UPR 2357, 67084 Strasbourg, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Strasbourg, Institut de Biologie Moléculaire Des Plantes (IBMP), CNRS-UPR 2357, 67084 Strasbourg</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Alsace (région administrative)</region><settlement type="city">Strasbourg</settlement></placeName><orgName type="university">Université de Strasbourg</orgName></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Champenoux</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Esposito, Sergio" sort="Esposito, Sergio" uniqKey="Esposito S" first="Sergio" last="Esposito">Sergio Esposito</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy. Electronic address: sergio.esposito@unina.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli</wicri:regionArea><wicri:noRegion>I-80126 Napoli</wicri:noRegion></affiliation></author></analytic><series><title level="j">Plant science : an international journal of experimental plant biology</title><idno type="eISSN">1873-2259</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Cysteine (chemistry)</term><term>Cysteine (physiology)</term><term>Glucosephosphate Dehydrogenase (chemistry)</term><term>Glucosephosphate Dehydrogenase (metabolism)</term><term>Glucosephosphate Dehydrogenase (physiology)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>NADP (antagonists & inhibitors)</term><term>NADP (chemistry)</term><term>Oxidation-Reduction (MeSH)</term><term>Pentose Phosphate Pathway (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Plant Proteins (physiology)</term><term>Plastids (metabolism)</term><term>Populus (genetics)</term><term>Populus (metabolism)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (metabolism)</term><term>Thioredoxins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Cystéine (composition chimique)</term><term>Cystéine (physiologie)</term><term>Glucose 6-phosphate dehydrogenase (composition chimique)</term><term>Glucose 6-phosphate dehydrogenase (métabolisme)</term><term>Glucose 6-phosphate dehydrogenase (physiologie)</term><term>Motifs d'acides aminés (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>NADP (antagonistes et inhibiteurs)</term><term>NADP (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Plastes (métabolisme)</term><term>Populus (génétique)</term><term>Populus (métabolisme)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (métabolisme)</term><term>Protéines végétales (physiologie)</term><term>Sites de fixation (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (métabolisme)</term><term>Thiorédoxines (physiologie)</term><term>Voie des pentoses phosphates (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>NADP</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Glucosephosphate Dehydrogenase</term><term>NADP</term><term>Plant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucosephosphate Dehydrogenase</term><term>Plant Proteins</term><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Cysteine</term><term>Glucosephosphate Dehydrogenase</term><term>Plant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>NADP</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Glucose 6-phosphate dehydrogenase</term><term>NADP</term><term>Protéines végétales</term><term>Thiorédoxines</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="metabolism" xml:lang="en"><term>Plastids</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glucose 6-phosphate dehydrogenase</term><term>Plastes</term><term>Populus</term><term>Protéines recombinantes</term><term>Protéines végétales</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cystéine</term><term>Glucose 6-phosphate dehydrogenase</term><term>Protéines végétales</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Cloning, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Oxidation-Reduction</term><term>Pentose Phosphate Pathway</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Clonage moléculaire</term><term>Motifs d'acides aminés</term><term>Mutagenèse dirigée</term><term>Oxydoréduction</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Voie des pentoses phosphates</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A cDNA coding for a plastidic P2-type G6PDH isoform from poplar (Populus tremula x tremuloides) has been used to express and purify to homogeneity the mature recombinant protein with a N-terminus His-tag. The study of the kinetic properties of the recombinant enzyme showed an in vitro redox sensing modulation exerted by reduced DTT. The interaction with thioredoxins (TRXs) was then investigated. Five cysteine to serine variants (C145S - C175S - C183S - C195S - C242S) and a variant with a double substitution for Cys<sup>175</sup> and Cys<sup>183</sup> (C175S/C183S) have been generated, purified and biochemically characterized in order to investigate the specific role(s) of cysteines in terms of redox regulation and NADPH-dependent inhibition. Three cysteine residues (C<sup>145</sup>, C<sup>194</sup>, C<sup>242</sup>) are suggested to have a role in controlling the NADP<sup>+</sup> access to the active site, and in stabilizing the NADPH regulatory binding site. Our results also indicate that the regulatory disulfide involves residues Cys<sup>175</sup> and Cys<sup>183</sup> in a position similar to those of chloroplastic P1-G6PDHs, but the modulation is exerted primarily by TRX m-type, in contrast to P1-G6PDH, which is regulated by TRX f. This unexpected specificity indicates differences in the mechanism of regulation, and redox sensing of plastidic P2-G6PDH compared to chloroplastic P1-G6PDH in higher plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27717462</PMID><DateCompleted><Year>2017</Year><Month>04</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2259</ISSN><JournalIssue CitedMedium="Internet"><Volume>252</Volume><PubDate><Year>2016</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Plant science : an international journal of experimental plant biology</Title><ISOAbbreviation>Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Plastidic P2 glucose-6P dehydrogenase from poplar is modulated by thioredoxin m-type: Distinct roles of cysteine residues in redox regulation and NADPH inhibition.</ArticleTitle><Pagination><MedlinePgn>257-266</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0168-9452(16)30289-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.plantsci.2016.08.003</ELocationID><Abstract><AbstractText>A cDNA coding for a plastidic P2-type G6PDH isoform from poplar (Populus tremula x tremuloides) has been used to express and purify to homogeneity the mature recombinant protein with a N-terminus His-tag. The study of the kinetic properties of the recombinant enzyme showed an in vitro redox sensing modulation exerted by reduced DTT. The interaction with thioredoxins (TRXs) was then investigated. Five cysteine to serine variants (C145S - C175S - C183S - C195S - C242S) and a variant with a double substitution for Cys<sup>175</sup> and Cys<sup>183</sup> (C175S/C183S) have been generated, purified and biochemically characterized in order to investigate the specific role(s) of cysteines in terms of redox regulation and NADPH-dependent inhibition. Three cysteine residues (C<sup>145</sup>, C<sup>194</sup>, C<sup>242</sup>) are suggested to have a role in controlling the NADP<sup>+</sup> access to the active site, and in stabilizing the NADPH regulatory binding site. Our results also indicate that the regulatory disulfide involves residues Cys<sup>175</sup> and Cys<sup>183</sup> in a position similar to those of chloroplastic P1-G6PDHs, but the modulation is exerted primarily by TRX m-type, in contrast to P1-G6PDH, which is regulated by TRX f. This unexpected specificity indicates differences in the mechanism of regulation, and redox sensing of plastidic P2-G6PDH compared to chloroplastic P1-G6PDH in higher plants.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier Ireland Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cardi</LastName><ForeName>Manuela</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zaffagnini</LastName><ForeName>Mirko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Dipartimento di Farmacia e Biotecnologie, Univ. di Bologna, I-40126 Bologna, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>De Lillo</LastName><ForeName>Alessia</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Castiglia</LastName><ForeName>Daniela</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chibani</LastName><ForeName>Kamel</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gualberto</LastName><ForeName>José Manuel</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Université de Strasbourg, Institut de Biologie Moléculaire Des Plantes (IBMP), CNRS-UPR 2357, 67084 Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Université de Lorraine, UMR 1136 Interactions Arbres/Microorganismes, Faculté des Sciences et Technologies, 54506, Vandoeuvre-lès-Nancy, France; INRA, UMR 1136 Interactions Arbres/Microorganismes, Centre INRA Nancy Lorraine, 54280, Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Esposito</LastName><ForeName>Sergio</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Dipartimento di Biologia, Univ. di Napoli "Federico II", I-80126 Napoli, Italy. Electronic address: sergio.esposito@unina.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>08</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Ireland</Country><MedlineTA>Plant Sci</MedlineTA><NlmUniqueID>9882015</NlmUniqueID><ISSNLinking>0168-9452</ISSNLinking></MedlineJournalInfo><ChemicalList><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>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.49</RegistryNumber><NameOfSubstance UI="D005954">Glucosephosphate Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005954" MajorTopicYN="N">Glucosephosphate Dehydrogenase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010427" MajorTopicYN="N">Pentose Phosphate Pathway</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018087" MajorTopicYN="N">Plastids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Cysteine</Keyword><Keyword MajorTopicYN="Y">Oxidative pentose phosphate pathway</Keyword><Keyword MajorTopicYN="Y">Populus</Keyword><Keyword MajorTopicYN="Y">Thioredoxins</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>06</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>08</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>08</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>10</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>10</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>4</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27717462</ArticleId><ArticleId IdType="pii">S0168-9452(16)30289-8</ArticleId><ArticleId IdType="doi">10.1016/j.plantsci.2016.08.003</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li><li>Italie</li></country><region><li>Alsace (région administrative)</li><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Champenoux</li><li>Strasbourg</li></settlement><orgName><li>Université de Lorraine</li><li>Université de Strasbourg</li></orgName></list><tree><country name="Italie"><noRegion><name sortKey="Cardi, Manuela" sort="Cardi, Manuela" uniqKey="Cardi M" first="Manuela" last="Cardi">Manuela Cardi</name></noRegion><name sortKey="Castiglia, Daniela" sort="Castiglia, Daniela" uniqKey="Castiglia D" first="Daniela" last="Castiglia">Daniela Castiglia</name><name sortKey="De Lillo, Alessia" sort="De Lillo, Alessia" uniqKey="De Lillo A" first="Alessia" last="De Lillo">Alessia De Lillo</name><name sortKey="Esposito, Sergio" sort="Esposito, Sergio" uniqKey="Esposito S" first="Sergio" last="Esposito">Sergio Esposito</name><name sortKey="Zaffagnini, Mirko" sort="Zaffagnini, Mirko" uniqKey="Zaffagnini M" first="Mirko" last="Zaffagnini">Mirko Zaffagnini</name></country><country name="France"><region name="Grand Est"><name sortKey="Chibani, Kamel" sort="Chibani, Kamel" uniqKey="Chibani K" first="Kamel" last="Chibani">Kamel Chibani</name></region><name sortKey="Gualberto, Jose Manuel" sort="Gualberto, Jose Manuel" uniqKey="Gualberto J" first="José Manuel" last="Gualberto">José Manuel Gualberto</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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