Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction.
Identifieur interne : 004456 ( Main/Exploration ); précédent : 004455; suivant : 004457Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction.
Auteurs : Eric Gelhaye [France] ; Nicolas Rouhier ; Jean Pierre JacquotSource :
- FEBS letters [ 0014-5793 ] ; 2003.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Disulfures (composition chimique), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Glutathion (métabolisme), Glutathione reductase (métabolisme), NADP (métabolisme), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Phylogenèse (MeSH), Populus (génétique), Populus (métabolisme), Protéines (métabolisme), Protéines Escherichia coli (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxine h (MeSH), Thiorédoxines (génétique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Disulfures.
- génétique : Populus, Protéines recombinantes, Thiorédoxines.
- métabolisme : Disulfures, Glutathion, Glutathione reductase, NADP, Populus, Protéines, Protéines Escherichia coli, Protéines recombinantes, Thioredoxin-disulfide reductase, Thiorédoxines.
- Alignement de séquences, Données de séquences moléculaires, Glutarédoxines, Oxidoreductases, Oxydoréduction, Phylogenèse, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Thiorédoxine h.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Disulfides (chemistry), Disulfides (metabolism), Escherichia coli Proteins (metabolism), Glutaredoxins (MeSH), Glutathione (metabolism), Glutathione Reductase (metabolism), Molecular Sequence Data (MeSH), NADP (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Phylogeny (MeSH), Populus (genetics), Populus (metabolism), Proteins (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Thioredoxin h (MeSH), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (genetics), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Disulfides.
- chemical , genetics : Recombinant Proteins, Thioredoxins.
- chemical , metabolism : Disulfides, Escherichia coli Proteins, Glutathione, Glutathione Reductase, NADP, Proteins, Recombinant Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- genetics : Populus.
- metabolism : Populus.
- Amino Acid Sequence, Glutaredoxins, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases, Phylogeny, Sequence Alignment, Sequence Homology, Amino Acid, Thioredoxin h.
Abstract
Poplar thioredoxin h4 (popTrxh4) and a related CXXS type (popCXXS3) are both members of a plant thioredoxin h subgroup. PopTrxh4 exhibits the usual catalytic site WCGPC, whereas popCXXS3 harbors the non-typical active site WCMPS. Recombinant popTrxh4 and popCXXS3 are not reduced either by Arabidopsis thaliana NADPH-dependent thioredoxin reductases (NTR) A and B or by Escherichia coli NTR. We report here evidence that a poplar glutaredoxin as well as three E. coli Grxs are able to reduce popTrxh4. PopTrxh4 is able to reduce several thioredoxin targets as peroxiredoxins or methionine sulfoxide reductases. On the other hand, popCXXS3 exhibits an activity in the presence of glutathione and hydroxyethyldisulfide. Except for examples of glutathiolation, these are the first two examples of a direct interconnection between the thioredoxin and glutathione/glutaredoxin systems.
DOI: 10.1016/s0014-5793(03)01301-2
PubMed: 14675753
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxine h (MeSH)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Escherichia coli Proteins</term><term>Glutathione</term><term>Glutathione Reductase</term><term>NADP</term><term>Proteins</term><term>Recombinant Proteins</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="composition 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Alignment</term><term>Sequence Homology, Amino Acid</term><term>Thioredoxin h</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Phylogenèse</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Thiorédoxine h</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Poplar thioredoxin h4 (popTrxh4) and a related CXXS type (popCXXS3) are both members of a plant thioredoxin h subgroup. PopTrxh4 exhibits the usual catalytic site WCGPC, whereas popCXXS3 harbors the non-typical active site WCMPS. Recombinant popTrxh4 and popCXXS3 are not reduced either by Arabidopsis thaliana NADPH-dependent thioredoxin reductases (NTR) A and B or by Escherichia coli NTR. We report here evidence that a poplar glutaredoxin as well as three E. coli Grxs are able to reduce popTrxh4. PopTrxh4 is able to reduce several thioredoxin targets as peroxiredoxins or methionine sulfoxide reductases. On the other hand, popCXXS3 exhibits an activity in the presence of glutathione and hydroxyethyldisulfide. Except for examples of glutathiolation, these are the first two examples of a direct interconnection between the thioredoxin and glutathione/glutaredoxin systems.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14675753</PMID><DateCompleted><Year>2004</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>555</Volume><Issue>3</Issue><PubDate><Year>2003</Year><Month>Dec</Month><Day>18</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Evidence for a subgroup of thioredoxin h that requires GSH/Grx for its reduction.</ArticleTitle><Pagination><MedlinePgn>443-8</MedlinePgn></Pagination><Abstract><AbstractText>Poplar thioredoxin h4 (popTrxh4) and a related CXXS type (popCXXS3) are both members of a plant thioredoxin h subgroup. PopTrxh4 exhibits the usual catalytic site WCGPC, whereas popCXXS3 harbors the non-typical active site WCMPS. Recombinant popTrxh4 and popCXXS3 are not reduced either by Arabidopsis thaliana NADPH-dependent thioredoxin reductases (NTR) A and B or by Escherichia coli NTR. We report here evidence that a poplar glutaredoxin as well as three E. coli Grxs are able to reduce popTrxh4. PopTrxh4 is able to reduce several thioredoxin targets as peroxiredoxins or methionine sulfoxide reductases. On the other hand, popCXXS3 exhibits an activity in the presence of glutathione and hydroxyethyldisulfide. Except for examples of glutathiolation, these are the first two examples of a direct interconnection between the thioredoxin and glutathione/glutaredoxin systems.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherche IaM INRA-UHP Nancy I, Université Henri Poincaré, 54506 Cedex, Vandoeuvre, France. gelhaye@lcb.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</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></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS 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MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029968" MajorTopicYN="N">Escherichia coli Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005980" MajorTopicYN="N">Glutathione Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054480" MajorTopicYN="N">Thioredoxin h</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>12</Month><Day>17</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>1</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>12</Month><Day>17</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14675753</ArticleId><ArticleId IdType="pii">S0014579303013012</ArticleId><ArticleId IdType="doi">10.1016/s0014-5793(03)01301-2</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Nancy</li></settlement><orgName><li>Université Henri Poincaré</li></orgName></list><tree><noCountry><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="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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