Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity.
Identifieur interne : 003279 ( Main/Exploration ); précédent : 003278; suivant : 003280Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity.
Auteurs : Jérémy Couturier [France] ; Claude Didierjean ; Jean-Pierre Jacquot ; Nicolas RouhierSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2010.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Fer (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Ingénierie des protéines (MeSH), Liaison aux protéines (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Populus (enzymologie), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Soufre (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Oxidoreductases, Protéines recombinantes.
- enzymologie : Populus.
- génétique : Glutarédoxines, Oxidoreductases, Protéines recombinantes.
- métabolisme : Fer, Glutarédoxines, Oxidoreductases, Protéines recombinantes, Soufre.
- Conformation des protéines, Données de séquences moléculaires, Ingénierie des protéines, Liaison aux protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Iron (metabolism), Molecular Sequence Data (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Populus (enzymology), Protein Binding (MeSH), Protein Conformation (MeSH), Protein Engineering (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sulfur (metabolism).
- MESH :
- chemical , chemistry : Glutaredoxins, Oxidoreductases, Recombinant Proteins.
- chemical , genetics : Glutaredoxins, Oxidoreductases, Recombinant Proteins.
- chemical , metabolism : Glutaredoxins, Iron, Oxidoreductases, Recombinant Proteins, Sulfur.
- enzymology : Populus.
- Amino Acid Sequence, Molecular Sequence Data, Protein Binding, Protein Conformation, Protein Engineering.
Abstract
In order to gather biochemical information about class III glutaredoxins (CCxC/S active sites), the active sites of two poplar class I glutaredoxins, GrxC1 and C4, CGYC and CPYC, respectively, were transformed into CCMC or CCMS. All the recombinant mutated proteins bind [2Fe-2S] centers into holodimers, whereas monomeric apoforms possess glutathione-dependent reductase activity. The functionally important, hydrophobic GALWL C-terminal end, found in most class III glutaredoxins, prevents expression in Escherichia coli. Changing the C-terminal end of GrxS7.2, a genuine class III glutaredoxin, allowed purifying some holoproteins. These properties are discussed considering the documented function of class III glutaredoxins in development.
DOI: 10.1016/j.bbrc.2010.11.050
PubMed: 21094149
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Populus (enzymologie)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Soufre (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Iron</term><term>Oxidoreductases</term><term>Recombinant Proteins</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="composition chimique" 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All the recombinant mutated proteins bind [2Fe-2S] centers into holodimers, whereas monomeric apoforms possess glutathione-dependent reductase activity. The functionally important, hydrophobic GALWL C-terminal end, found in most class III glutaredoxins, prevents expression in Escherichia coli. Changing the C-terminal end of GrxS7.2, a genuine class III glutaredoxin, allowed purifying some holoproteins. 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All the recombinant mutated proteins bind [2Fe-2S] centers into holodimers, whereas monomeric apoforms possess glutathione-dependent reductase activity. The functionally important, hydrophobic GALWL C-terminal end, found in most class III glutaredoxins, prevents expression in Escherichia coli. Changing the C-terminal end of GrxS7.2, a genuine class III glutaredoxin, allowed purifying some holoproteins. These properties are discussed considering the documented function of class III glutaredoxins in development.</AbstractText><CopyrightInformation>Copyright © 2010 Elsevier Inc. 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IdType="doi">10.1016/j.bbrc.2010.11.050</ArticleId></ArticleIdList></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="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</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></noCountry><country name="France"><region name="Grand Est"><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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