Biochemical properties of poplar thioredoxin z.
Identifieur interne : 002E93 ( Main/Corpus ); précédent : 002E92; suivant : 002E94Biochemical properties of poplar thioredoxin z.
Auteurs : Kamel Chibani ; Lionel Tarrago ; Peter Schürmann ; Jean-Pierre Jacquot ; Nicolas RouhierSource :
- FEBS letters [ 1873-3468 ] ; 2011.
English descriptors
- KwdEn :
- Antioxidants (metabolism), Electron Transport (MeSH), Iron-Sulfur Proteins (metabolism), Oxidoreductases (metabolism), Plant Proteins (metabolism), Plastids (metabolism), Populus (cytology), Populus (enzymology), Populus (metabolism), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : Antioxidants, Iron-Sulfur Proteins, Oxidoreductases, Plant Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- cytology : Populus.
- enzymology : Populus.
- metabolism : Plastids, Populus.
- Electron Transport.
Abstract
Trx-z is a chloroplastic thioredoxin, exhibiting a usual WCGPC active site, but whose biochemical properties are unknown. We demonstrate here that Trx-z supports the activity of several plastidial antioxidant enzymes, such as thiol-peroxidases and methionine sulfoxide reductases, using electrons provided by ferredoxin-thioredoxin reductase. Its disulfide reductase activity requires the presence of both active site cysteines forming a catalytic disulfide bridge with a midpoint redox potential of -251 mV at pH7. These in vitro biochemical data suggest that, besides its decisive role in the regulation of plastidial transcription, Trx-z might also be involved in stress response.
DOI: 10.1016/j.febslet.2011.03.006
PubMed: 21385584
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pubmed:21385584Le document en format XML
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<author><name sortKey="Chibani, Kamel" sort="Chibani, Kamel" uniqKey="Chibani K" first="Kamel" last="Chibani">Kamel Chibani</name>
<affiliation><nlm:affiliation>UMR 1136 INRA Nancy University, Interactions Arbres-Microorganismes, IFR 110 EFABA, Faculté des Sciences, 54506 Vandœuvre-lès-Nancy, France.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Tarrago, Lionel" sort="Tarrago, Lionel" uniqKey="Tarrago L" first="Lionel" last="Tarrago">Lionel Tarrago</name>
</author>
<author><name sortKey="Schurmann, Peter" sort="Schurmann, Peter" uniqKey="Schurmann P" first="Peter" last="Schürmann">Peter Schürmann</name>
</author>
<author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name>
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<author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Biochemical properties of poplar thioredoxin z.</title>
<author><name sortKey="Chibani, Kamel" sort="Chibani, Kamel" uniqKey="Chibani K" first="Kamel" last="Chibani">Kamel Chibani</name>
<affiliation><nlm:affiliation>UMR 1136 INRA Nancy University, Interactions Arbres-Microorganismes, IFR 110 EFABA, Faculté des Sciences, 54506 Vandœuvre-lès-Nancy, France.</nlm:affiliation>
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<author><name sortKey="Tarrago, Lionel" sort="Tarrago, Lionel" uniqKey="Tarrago L" first="Lionel" last="Tarrago">Lionel Tarrago</name>
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<author><name sortKey="Schurmann, Peter" sort="Schurmann, Peter" uniqKey="Schurmann P" first="Peter" last="Schürmann">Peter Schürmann</name>
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<series><title level="j">FEBS letters</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antioxidants (metabolism)</term>
<term>Electron Transport (MeSH)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Plant Proteins (metabolism)</term>
<term>Plastids (metabolism)</term>
<term>Populus (cytology)</term>
<term>Populus (enzymology)</term>
<term>Populus (metabolism)</term>
<term>Thioredoxin-Disulfide Reductase (metabolism)</term>
<term>Thioredoxins (metabolism)</term>
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<term>Iron-Sulfur Proteins</term>
<term>Oxidoreductases</term>
<term>Plant Proteins</term>
<term>Thioredoxin-Disulfide Reductase</term>
<term>Thioredoxins</term>
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<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Populus</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plastids</term>
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<front><div type="abstract" xml:lang="en">Trx-z is a chloroplastic thioredoxin, exhibiting a usual WCGPC active site, but whose biochemical properties are unknown. We demonstrate here that Trx-z supports the activity of several plastidial antioxidant enzymes, such as thiol-peroxidases and methionine sulfoxide reductases, using electrons provided by ferredoxin-thioredoxin reductase. Its disulfide reductase activity requires the presence of both active site cysteines forming a catalytic disulfide bridge with a midpoint redox potential of -251 mV at pH7. These in vitro biochemical data suggest that, besides its decisive role in the regulation of plastidial transcription, Trx-z might also be involved in stress response.</div>
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<Abstract><AbstractText>Trx-z is a chloroplastic thioredoxin, exhibiting a usual WCGPC active site, but whose biochemical properties are unknown. We demonstrate here that Trx-z supports the activity of several plastidial antioxidant enzymes, such as thiol-peroxidases and methionine sulfoxide reductases, using electrons provided by ferredoxin-thioredoxin reductase. Its disulfide reductase activity requires the presence of both active site cysteines forming a catalytic disulfide bridge with a midpoint redox potential of -251 mV at pH7. These in vitro biochemical data suggest that, besides its decisive role in the regulation of plastidial transcription, Trx-z might also be involved in stress response.</AbstractText>
<CopyrightInformation>Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</CopyrightInformation>
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<ForeName>Kamel</ForeName>
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