Thioredoxins and related proteins in photosynthetic organisms: molecular basis for thiol dependent regulation.
Identifieur interne : 000F61 ( Main/Exploration ); précédent : 000F60; suivant : 000F62Thioredoxins and related proteins in photosynthetic organisms: molecular basis for thiol dependent regulation.
Auteurs : Jean-Pierre Jacquot [France] ; Eric Gelhaye ; Nicolas Rouhier ; Catherine Corbier ; Claude Didierjean ; André AubrySource :
- Biochemical pharmacology [ 0006-2952 ] ; 2002.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Catalyse (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Photosynthèse (physiologie), Plantes (MeSH), Protein Disulfide-Isomerases (métabolisme), Protein-disulfide reductase (glutathione) (métabolisme), Protéines (métabolisme), Prévision (MeSH), Thiols (métabolisme), Thiorédoxines (métabolisme).
- MESH :
- métabolisme : Peroxidases, Protein Disulfide-Isomerases, Protein-disulfide reductase (glutathione), Protéines, Thiols, Thiorédoxines.
- physiologie : Photosynthèse.
- Animaux, Catalyse, Glutarédoxines, Humains, Modèles moléculaires, Oxidoreductases, Oxydoréduction, Peroxirédoxines, Plantes, Prévision.
English descriptors
- KwdEn :
- Animals (MeSH), Catalysis (MeSH), Forecasting (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Peroxidases (metabolism), Peroxiredoxins (MeSH), Photosynthesis (physiology), Plants (MeSH), Protein Disulfide Reductase (Glutathione) (metabolism), Protein Disulfide-Isomerases (metabolism), Proteins (metabolism), Sulfhydryl Compounds (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : Peroxidases, Protein Disulfide Reductase (Glutathione), Protein Disulfide-Isomerases, Proteins, Sulfhydryl Compounds, Thioredoxins.
- chemical : Glutaredoxins, Oxidoreductases, Peroxiredoxins.
- physiology : Photosynthesis.
- Animals, Catalysis, Forecasting, Humans, Models, Molecular, Oxidation-Reduction, Plants.
Abstract
Thioredoxins are small molecular weight disulfide oxidoreductases specialized in the reduction of disulfide bonds on other proteins. Generally, the enzymes which are selectively and reversibly reduced by these proteins oscillate between an oxidized and inactive conformation and a reduced and active conformation. Thioredoxin constitutes the archetype of a family of protein disulfide oxidoreductases which comprises glutaredoxin and protein disulfide isomerase. Thioredoxin and glutaredoxin serve many roles in the cell, including the redox regulation of target enzymes and transcription factors. They can also serve as hydrogen donors to peroxiredoxins, recently discovered heme free peroxidases, the function of which is to get rid of hydroperoxides in the cell. This review describes the molecular basis for the functioning and interaction between these enzymes in photosynthetic organisms.
DOI: 10.1016/s0006-2952(02)01177-2
PubMed: 12213606
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Catalyse (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (métabolisme)</term><term>Peroxirédoxines (MeSH)</term><term>Photosynthèse (physiologie)</term><term>Plantes (MeSH)</term><term>Protein Disulfide-Isomerases (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (métabolisme)</term><term>Protéines (métabolisme)</term><term>Prévision (MeSH)</term><term>Thiols (métabolisme)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peroxidases</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Protein Disulfide-Isomerases</term><term>Proteins</term><term>Sulfhydryl Compounds</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" 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Generally, the enzymes which are selectively and reversibly reduced by these proteins oscillate between an oxidized and inactive conformation and a reduced and active conformation. Thioredoxin constitutes the archetype of a family of protein disulfide oxidoreductases which comprises glutaredoxin and protein disulfide isomerase. Thioredoxin and glutaredoxin serve many roles in the cell, including the redox regulation of target enzymes and transcription factors. They can also serve as hydrogen donors to peroxiredoxins, recently discovered heme free peroxidases, the function of which is to get rid of hydroperoxides in the cell. This review describes the molecular basis for the functioning and interaction between these enzymes in photosynthetic organisms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12213606</PMID><DateCompleted><Year>2002</Year><Month>10</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>23</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2952</ISSN><JournalIssue CitedMedium="Print"><Volume>64</Volume><Issue>5-6</Issue><PubDate><Year>2002</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Biochemical pharmacology</Title><ISOAbbreviation>Biochem Pharmacol</ISOAbbreviation></Journal><ArticleTitle>Thioredoxins and related proteins in photosynthetic organisms: molecular basis for thiol dependent regulation.</ArticleTitle><Pagination><MedlinePgn>1065-9</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxins are small molecular weight disulfide oxidoreductases specialized in the reduction of disulfide bonds on other proteins. Generally, the enzymes which are selectively and reversibly reduced by these proteins oscillate between an oxidized and inactive conformation and a reduced and active conformation. Thioredoxin constitutes the archetype of a family of protein disulfide oxidoreductases which comprises glutaredoxin and protein disulfide isomerase. Thioredoxin and glutaredoxin serve many roles in the cell, including the redox regulation of target enzymes and transcription factors. They can also serve as hydrogen donors to peroxiredoxins, recently discovered heme free peroxidases, the function of which is to get rid of hydroperoxides in the cell. This review describes the molecular basis for the functioning and interaction between these enzymes in photosynthetic organisms.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>UMR INRA UHP Interaction Arbres Microorganismes, Université Henri Poincaré, Vandoeuvre, France. j2p@scbiol.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Corbier</LastName><ForeName>Catherine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Aubry</LastName><ForeName>André</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem Pharmacol</MedlineTA><NlmUniqueID>0101032</NlmUniqueID><ISSNLinking>0006-2952</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019704" MajorTopicYN="N">Protein Disulfide-Isomerases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>53</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>9</Month><Day>6</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>10</Month><Day>18</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>9</Month><Day>6</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12213606</ArticleId><ArticleId IdType="pii">S0006295202011772</ArticleId><ArticleId IdType="doi">10.1016/s0006-2952(02)01177-2</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="Aubry, Andre" sort="Aubry, Andre" uniqKey="Aubry A" first="André" last="Aubry">André Aubry</name><name sortKey="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</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="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre 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