Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin.
Identifieur interne : 003E25 ( Main/Exploration ); précédent : 003E24; suivant : 003E26Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin.
Auteurs : Nicholas Rouhier [France] ; Filipe Gama ; Gunnar Wingsle ; Eric Gelhaye ; Pierre Gans ; Jean-Pierre JacquotSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2006.
Descripteurs français
- KwdFr :
- Dichroïsme circulaire (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Glutathion (métabolisme), Ingénierie des protéines (méthodes), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Peroxidases (génétique), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Populus (enzymologie), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Thiorédoxines (génétique), Thiorédoxines (métabolisme).
- MESH :
- enzymologie : Populus.
- génétique : Oxidoreductases, Peroxidases, Protéines de fusion recombinantes, Thiorédoxines.
- métabolisme : Glutathion, Oxidoreductases, Peroxidases, Protéines de fusion recombinantes, Thiorédoxines.
- méthodes : Ingénierie des protéines.
- Dichroïsme circulaire, Données de séquences moléculaires, Glutarédoxines, Oxydoréduction, Peroxirédoxines, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Circular Dichroism (MeSH), Glutaredoxins (MeSH), Glutathione (metabolism), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism), Peroxidases (genetics), Peroxidases (metabolism), Peroxiredoxins (MeSH), Populus (enzymology), Protein Engineering (methods), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Thioredoxins (genetics), Thioredoxins (metabolism).
- MESH :
- chemical , genetics : Oxidoreductases, Peroxidases, Recombinant Fusion Proteins, Thioredoxins.
- chemical , metabolism : Glutathione, Oxidoreductases, Peroxidases, Recombinant Fusion Proteins, Thioredoxins.
- chemical : Glutaredoxins, Peroxiredoxins.
- enzymology : Populus.
- methods : Protein Engineering.
- Amino Acid Sequence, Base Sequence, Circular Dichroism, Molecular Sequence Data, Oxidation-Reduction.
Abstract
The existence of natural peroxiredoxin-glutaredoxin hybrid enzymes in several bacteria is in line with previous findings indicating that poplar peroxiredoxin II can use glutaredoxin as an electron donor. This peroxiredoxin remains however unique since it also uses thioredoxin with a quite good efficiency. Based on the existing fusions, we have created artificial enzymes containing a poplar peroxiredoxin module linked to glutaredoxin or thioredoxin modules. The recombinant fusion enzymes folded properly into non-covalently bound homodimers or homotetramers. Two of the three protein constructs exhibit peroxidase activity, a reaction where the two modules need to function together, but they also display enzymatic activities specific of each module. In addition, mass spectrometry analyses indicate that the Prx module can be both glutathiolated or overoxidized in vitro. This is discussed in the light of the Prx reactivity.
DOI: 10.1016/j.bbrc.2006.01.099
PubMed: 16476584
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xml:lang="fr"><term>Dichroïsme circulaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Ingénierie des protéines (méthodes)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Peroxirédoxines (MeSH)</term><term>Populus (enzymologie)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term><term>Peroxidases</term><term>Recombinant Fusion Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Oxidoreductases</term><term>Peroxidases</term><term>Recombinant Fusion Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Peroxiredoxins</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="génétique" xml:lang="fr"><term>Oxidoreductases</term><term>Peroxidases</term><term>Protéines de fusion recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Protein Engineering</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Oxidoreductases</term><term>Peroxidases</term><term>Protéines de fusion recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Ingénierie des protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Circular Dichroism</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dichroïsme circulaire</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Oxydoréduction</term><term>Peroxirédoxines</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The existence of natural peroxiredoxin-glutaredoxin hybrid enzymes in several bacteria is in line with previous findings indicating that poplar peroxiredoxin II can use glutaredoxin as an electron donor. This peroxiredoxin remains however unique since it also uses thioredoxin with a quite good efficiency. Based on the existing fusions, we have created artificial enzymes containing a poplar peroxiredoxin module linked to glutaredoxin or thioredoxin modules. The recombinant fusion enzymes folded properly into non-covalently bound homodimers or homotetramers. Two of the three protein constructs exhibit peroxidase activity, a reaction where the two modules need to function together, but they also display enzymatic activities specific of each module. In addition, mass spectrometry analyses indicate that the Prx module can be both glutathiolated or overoxidized in vitro. This is discussed in the light of the Prx reactivity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16476584</PMID><DateCompleted><Year>2006</Year><Month>04</Month><Day>25</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>341</Volume><Issue>4</Issue><PubDate><Year>2006</Year><Month>Mar</Month><Day>24</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Engineering functional artificial hybrid proteins between poplar peroxiredoxin II and glutaredoxin or thioredoxin.</ArticleTitle><Pagination><MedlinePgn>1300-8</MedlinePgn></Pagination><Abstract><AbstractText>The existence of natural peroxiredoxin-glutaredoxin hybrid enzymes in several bacteria is in line with previous findings indicating that poplar peroxiredoxin II can use glutaredoxin as an electron donor. This peroxiredoxin remains however unique since it also uses thioredoxin with a quite good efficiency. Based on the existing fusions, we have created artificial enzymes containing a poplar peroxiredoxin module linked to glutaredoxin or thioredoxin modules. The recombinant fusion enzymes folded properly into non-covalently bound homodimers or homotetramers. Two of the three protein constructs exhibit peroxidase activity, a reaction where the two modules need to function together, but they also display enzymatic activities specific of each module. In addition, mass spectrometry analyses indicate that the Prx module can be both glutathiolated or overoxidized in vitro. This is discussed in the light of the Prx reactivity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicholas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>UMR 1136 Interactions Arbres Mircoorganismes INRA-UHP, IFR 110 GEEF, Faculté des Sciences, 54506 Vandouevre-les-Nancy Cedex, France. nrouhier@scbiol.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gama</LastName><ForeName>Filipe</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Wingsle</LastName><ForeName>Gunnar</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Gans</LastName><ForeName>Pierre</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</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="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" 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F" first="Filipe" last="Gama">Filipe Gama</name><name sortKey="Gans, Pierre" sort="Gans, Pierre" uniqKey="Gans P" first="Pierre" last="Gans">Pierre Gans</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Wingsle, Gunnar" sort="Wingsle, Gunnar" uniqKey="Wingsle G" first="Gunnar" last="Wingsle">Gunnar Wingsle</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Rouhier, Nicholas" sort="Rouhier, Nicholas" uniqKey="Rouhier N" first="Nicholas" last="Rouhier">Nicholas Rouhier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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