Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes.
Identifieur interne : 000B90 ( Main/Exploration ); précédent : 000B89; suivant : 000B91Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes.
Auteurs : Marcelo A. Comini [Allemagne] ; Jochen Rettig ; Natalie Dirdjaja ; Eva-Maria Hanschmann ; Carsten Berndt ; R Luise Krauth-SiegelSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cytosol (enzymologie), Déferoxamine (pharmacologie), Fer (métabolisme), Glutarédoxines (biosynthèse), Glutarédoxines (génétique), Humains (MeSH), Isoenzymes (biosynthèse), Isoenzymes (génétique), Maladie du sommeil (enzymologie), Maladie du sommeil (génétique), Ménadione (pharmacologie), Métalloprotéines (biosynthèse), Métalloprotéines (génétique), Oxydants (pharmacologie), Peroxyde d'hydrogène (pharmacologie), Protéines de protozoaire (biosynthèse), Protéines de protozoaire (génétique), Protéines mitochondriales (biosynthèse), Protéines mitochondriales (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (génétique), Régulation de l'expression des gènes codant pour des enzymes (effets des médicaments et des substances chimiques), Régulation de l'expression des gènes codant pour des enzymes (physiologie), Régulation positive (effets des médicaments et des substances chimiques), Régulation positive (physiologie), Sidérophores (pharmacologie), Soufre (métabolisme), Trypanosoma brucei brucei (enzymologie), Trypanosoma brucei brucei (génétique), Vitamines (pharmacologie).
- MESH :
- biosynthèse : Glutarédoxines, Isoenzymes, Métalloprotéines, Protéines de protozoaire, Protéines mitochondriales, Protéines recombinantes.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes codant pour des enzymes, Régulation positive.
- enzymologie : Cytosol, Maladie du sommeil, Trypanosoma brucei brucei.
- génétique : Glutarédoxines, Isoenzymes, Maladie du sommeil, Métalloprotéines, Protéines de protozoaire, Protéines mitochondriales, Protéines recombinantes, Trypanosoma brucei brucei.
- métabolisme : Fer, Soufre.
- pharmacologie : Déferoxamine, Ménadione, Oxydants, Peroxyde d'hydrogène, Sidérophores, Vitamines.
- physiologie : Régulation de l'expression des gènes codant pour des enzymes, Régulation positive.
- Animaux, Humains.
English descriptors
- KwdEn :
- Animals (MeSH), Cytosol (enzymology), Deferoxamine (pharmacology), Gene Expression Regulation, Enzymologic (drug effects), Gene Expression Regulation, Enzymologic (physiology), Glutaredoxins (biosynthesis), Glutaredoxins (genetics), Humans (MeSH), Hydrogen Peroxide (pharmacology), Iron (metabolism), Isoenzymes (biosynthesis), Isoenzymes (genetics), Metalloproteins (biosynthesis), Metalloproteins (genetics), Mitochondrial Proteins (biosynthesis), Mitochondrial Proteins (genetics), Oxidants (pharmacology), Protozoan Proteins (biosynthesis), Protozoan Proteins (genetics), Recombinant Proteins (biosynthesis), Recombinant Proteins (genetics), Siderophores (pharmacology), Sulfur (metabolism), Trypanosoma brucei brucei (enzymology), Trypanosoma brucei brucei (genetics), Trypanosomiasis, African (enzymology), Trypanosomiasis, African (genetics), Up-Regulation (drug effects), Up-Regulation (physiology), Vitamin K 3 (pharmacology), Vitamins (pharmacology).
- MESH :
- chemical , biosynthesis : Glutaredoxins, Isoenzymes, Metalloproteins, Mitochondrial Proteins, Protozoan Proteins, Recombinant Proteins.
- chemical , genetics : Glutaredoxins, Isoenzymes, Metalloproteins, Mitochondrial Proteins, Protozoan Proteins, Recombinant Proteins.
- chemical , metabolism : Iron, Sulfur.
- chemical , pharmacology : Deferoxamine, Hydrogen Peroxide, Oxidants, Siderophores, Vitamin K 3, Vitamins.
- drug effects : Gene Expression Regulation, Enzymologic, Up-Regulation.
- enzymology : Cytosol, Trypanosoma brucei brucei, Trypanosomiasis, African.
- genetics : Trypanosoma brucei brucei, Trypanosomiasis, African.
- physiology : Gene Expression Regulation, Enzymologic, Up-Regulation.
- Animals, Humans.
Abstract
African trypanosomes encode three monothiol glutaredoxins (1-C-Grx). 1-C-Grx1 occurs exclusively in the mitochondrion, and 1-C-Grx2 and -3 are predicted to be mitochondrial and cytosolic proteins, respectively. All three 1-C-Grx are expressed in both the mammalian bloodstream and the insect procyclic form of Trypanosoma brucei, with the highest levels found in stationary phase and starving parasites. In the rudimentary mitochondrion of bloodstream cells, 1-C-Grx1 reaches concentrations above 200 microm/subunit. Recombinant T. brucei 1-C-Grx1 exists as a noncovalent homodimer, whereas 1-C-Grx2 and 1-C-Grx3 are monomeric proteins. In vitro, dimeric 1-C-Grx1 coordinated an H(2)O(2)-sensitive [2Fe-2S] cluster that required GSH as an additional ligand. Both bloodstream and procyclic trypanosomes were refractory to down-regulation of 1-C-Grx1 expression by RNA interference. In procyclic parasites, the 1-c-grx1 alleles could only be deleted if an ectopic copy of the gene was expressed. A 5-10-fold overexpression of 1-C-Grx1 in both parasite forms did not yield a growth phenotype under optimal culture conditions. However, exposure of these cells to the iron chelator deferoxamine or H(2)O(2), but not to iron or menadione, impaired cell growth. Treatment of wild-type bloodstream parasites with deferoxamine and H(2)O(2) caused a 2-fold down- and up-regulation of 1-C-Grx1, respectively. The results point to an essential role of the mitochondrial 1-C-Grx1 in the iron metabolism of these parasites.
DOI: 10.1074/jbc.M802010200
PubMed: 18669638
Affiliations:
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Comini</name><affiliation wicri:level="3"><nlm:affiliation>Centre of Biochemistry, Heidelberg University, Im Neuenheimer Feld 504, D-69120 Heidelberg, Germany. mcomini@pateur.edu.uy</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Centre of Biochemistry, Heidelberg University, Im Neuenheimer Feld 504, D-69120 Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Rettig, Jochen" sort="Rettig, Jochen" uniqKey="Rettig J" first="Jochen" last="Rettig">Jochen Rettig</name></author><author><name sortKey="Dirdjaja, Natalie" sort="Dirdjaja, Natalie" uniqKey="Dirdjaja N" first="Natalie" last="Dirdjaja">Natalie Dirdjaja</name></author><author><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name></author><author><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name></author><author><name sortKey="Krauth Siegel, R Luise" sort="Krauth Siegel, R Luise" uniqKey="Krauth Siegel R" first="R Luise" last="Krauth-Siegel">R Luise Krauth-Siegel</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18669638</idno><idno type="pmid">18669638</idno><idno type="doi">10.1074/jbc.M802010200</idno><idno type="wicri:Area/Main/Corpus">000B70</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B70</idno><idno type="wicri:Area/Main/Curation">000B70</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B70</idno><idno type="wicri:Area/Main/Exploration">000B70</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes.</title><author><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. 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last="Hanschmann">Eva-Maria Hanschmann</name></author><author><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name></author><author><name sortKey="Krauth Siegel, R Luise" sort="Krauth Siegel, R Luise" uniqKey="Krauth Siegel R" first="R Luise" last="Krauth-Siegel">R Luise Krauth-Siegel</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cytosol (enzymology)</term><term>Deferoxamine (pharmacology)</term><term>Gene Expression Regulation, Enzymologic (drug effects)</term><term>Gene Expression Regulation, Enzymologic (physiology)</term><term>Glutaredoxins (biosynthesis)</term><term>Glutaredoxins (genetics)</term><term>Humans (MeSH)</term><term>Hydrogen Peroxide (pharmacology)</term><term>Iron (metabolism)</term><term>Isoenzymes (biosynthesis)</term><term>Isoenzymes (genetics)</term><term>Metalloproteins (biosynthesis)</term><term>Metalloproteins (genetics)</term><term>Mitochondrial Proteins (biosynthesis)</term><term>Mitochondrial Proteins (genetics)</term><term>Oxidants (pharmacology)</term><term>Protozoan Proteins (biosynthesis)</term><term>Protozoan Proteins (genetics)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (genetics)</term><term>Siderophores (pharmacology)</term><term>Sulfur (metabolism)</term><term>Trypanosoma brucei brucei (enzymology)</term><term>Trypanosoma brucei brucei (genetics)</term><term>Trypanosomiasis, African (enzymology)</term><term>Trypanosomiasis, African (genetics)</term><term>Up-Regulation (drug effects)</term><term>Up-Regulation (physiology)</term><term>Vitamin K 3 (pharmacology)</term><term>Vitamins (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cytosol (enzymologie)</term><term>Déferoxamine (pharmacologie)</term><term>Fer (métabolisme)</term><term>Glutarédoxines (biosynthèse)</term><term>Glutarédoxines (génétique)</term><term>Humains (MeSH)</term><term>Isoenzymes (biosynthèse)</term><term>Isoenzymes (génétique)</term><term>Maladie du sommeil (enzymologie)</term><term>Maladie du sommeil (génétique)</term><term>Ménadione (pharmacologie)</term><term>Métalloprotéines (biosynthèse)</term><term>Métalloprotéines (génétique)</term><term>Oxydants (pharmacologie)</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Protéines de protozoaire (biosynthèse)</term><term>Protéines de protozoaire (génétique)</term><term>Protéines mitochondriales (biosynthèse)</term><term>Protéines mitochondriales (génétique)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (génétique)</term><term>Régulation de l'expression des gènes codant pour des enzymes (effets des médicaments et des substances chimiques)</term><term>Régulation de l'expression des gènes codant pour des enzymes (physiologie)</term><term>Régulation positive (effets des médicaments et des substances chimiques)</term><term>Régulation positive (physiologie)</term><term>Sidérophores (pharmacologie)</term><term>Soufre (métabolisme)</term><term>Trypanosoma brucei brucei (enzymologie)</term><term>Trypanosoma brucei brucei (génétique)</term><term>Vitamines (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Glutaredoxins</term><term>Isoenzymes</term><term>Metalloproteins</term><term>Mitochondrial Proteins</term><term>Protozoan Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Isoenzymes</term><term>Metalloproteins</term><term>Mitochondrial Proteins</term><term>Protozoan Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Iron</term><term>Sulfur</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Deferoxamine</term><term>Hydrogen Peroxide</term><term>Oxidants</term><term>Siderophores</term><term>Vitamin K 3</term><term>Vitamins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glutarédoxines</term><term>Isoenzymes</term><term>Métalloprotéines</term><term>Protéines de protozoaire</term><term>Protéines mitochondriales</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gene Expression Regulation, Enzymologic</term><term>Up-Regulation</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Régulation positive</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cytosol</term><term>Maladie du sommeil</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cytosol</term><term>Trypanosoma brucei brucei</term><term>Trypanosomiasis, African</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Trypanosoma brucei brucei</term><term>Trypanosomiasis, African</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Isoenzymes</term><term>Maladie du sommeil</term><term>Métalloprotéines</term><term>Protéines de protozoaire</term><term>Protéines mitochondriales</term><term>Protéines recombinantes</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fer</term><term>Soufre</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Déferoxamine</term><term>Ménadione</term><term>Oxydants</term><term>Peroxyde d'hydrogène</term><term>Sidérophores</term><term>Vitamines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Régulation positive</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Enzymologic</term><term>Up-Regulation</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">African trypanosomes encode three monothiol glutaredoxins (1-C-Grx). 1-C-Grx1 occurs exclusively in the mitochondrion, and 1-C-Grx2 and -3 are predicted to be mitochondrial and cytosolic proteins, respectively. All three 1-C-Grx are expressed in both the mammalian bloodstream and the insect procyclic form of Trypanosoma brucei, with the highest levels found in stationary phase and starving parasites. In the rudimentary mitochondrion of bloodstream cells, 1-C-Grx1 reaches concentrations above 200 microm/subunit. Recombinant T. brucei 1-C-Grx1 exists as a noncovalent homodimer, whereas 1-C-Grx2 and 1-C-Grx3 are monomeric proteins. In vitro, dimeric 1-C-Grx1 coordinated an H(2)O(2)-sensitive [2Fe-2S] cluster that required GSH as an additional ligand. Both bloodstream and procyclic trypanosomes were refractory to down-regulation of 1-C-Grx1 expression by RNA interference. In procyclic parasites, the 1-c-grx1 alleles could only be deleted if an ectopic copy of the gene was expressed. A 5-10-fold overexpression of 1-C-Grx1 in both parasite forms did not yield a growth phenotype under optimal culture conditions. However, exposure of these cells to the iron chelator deferoxamine or H(2)O(2), but not to iron or menadione, impaired cell growth. Treatment of wild-type bloodstream parasites with deferoxamine and H(2)O(2) caused a 2-fold down- and up-regulation of 1-C-Grx1, respectively. The results point to an essential role of the mitochondrial 1-C-Grx1 in the iron metabolism of these parasites.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18669638</PMID><DateCompleted><Year>2008</Year><Month>11</Month><Day>10</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>41</Issue><PubDate><Year>2008</Year><Month>Oct</Month><Day>10</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes.</ArticleTitle><Pagination><MedlinePgn>27785-98</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M802010200</ELocationID><Abstract><AbstractText>African trypanosomes encode three monothiol glutaredoxins (1-C-Grx). 1-C-Grx1 occurs exclusively in the mitochondrion, and 1-C-Grx2 and -3 are predicted to be mitochondrial and cytosolic proteins, respectively. All three 1-C-Grx are expressed in both the mammalian bloodstream and the insect procyclic form of Trypanosoma brucei, with the highest levels found in stationary phase and starving parasites. In the rudimentary mitochondrion of bloodstream cells, 1-C-Grx1 reaches concentrations above 200 microm/subunit. Recombinant T. brucei 1-C-Grx1 exists as a noncovalent homodimer, whereas 1-C-Grx2 and 1-C-Grx3 are monomeric proteins. In vitro, dimeric 1-C-Grx1 coordinated an H(2)O(2)-sensitive [2Fe-2S] cluster that required GSH as an additional ligand. Both bloodstream and procyclic trypanosomes were refractory to down-regulation of 1-C-Grx1 expression by RNA interference. In procyclic parasites, the 1-c-grx1 alleles could only be deleted if an ectopic copy of the gene was expressed. A 5-10-fold overexpression of 1-C-Grx1 in both parasite forms did not yield a growth phenotype under optimal culture conditions. However, exposure of these cells to the iron chelator deferoxamine or H(2)O(2), but not to iron or menadione, impaired cell growth. Treatment of wild-type bloodstream parasites with deferoxamine and H(2)O(2) caused a 2-fold down- and up-regulation of 1-C-Grx1, respectively. The results point to an essential role of the mitochondrial 1-C-Grx1 in the iron metabolism of these parasites.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Centre of Biochemistry, Heidelberg University, Im Neuenheimer Feld 504, D-69120 Heidelberg, Germany. mcomini@pateur.edu.uy</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rettig</LastName><ForeName>Jochen</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Dirdjaja</LastName><ForeName>Natalie</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Hanschmann</LastName><ForeName>Eva-Maria</ForeName><Initials>EM</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Krauth-Siegel</LastName><ForeName>R Luise</ForeName><Initials>RL</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><ArticleDate DateType="Electronic"><Year>2008</Year><Month>07</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008667">Metalloproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016877">Oxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015800">Protozoan Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017262">Siderophores</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014815">Vitamins</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>723JX6CXY5</RegistryNumber><NameOfSubstance UI="D024483">Vitamin K 3</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>J06Y7MXW4D</RegistryNumber><NameOfSubstance UI="D003676">Deferoxamine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003676" MajorTopicYN="N">Deferoxamine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" 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African</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015854" MajorTopicYN="N">Up-Regulation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024483" MajorTopicYN="N">Vitamin K 3</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014815" MajorTopicYN="N">Vitamins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>8</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>11</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>8</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18669638</ArticleId><ArticleId IdType="pii">M802010200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M802010200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bade-Wurtemberg</li><li>District de Karlsruhe</li></region><settlement><li>Heidelberg</li></settlement></list><tree><noCountry><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name><name sortKey="Dirdjaja, Natalie" sort="Dirdjaja, Natalie" uniqKey="Dirdjaja N" first="Natalie" last="Dirdjaja">Natalie Dirdjaja</name><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name><name sortKey="Krauth Siegel, R Luise" sort="Krauth Siegel, R Luise" uniqKey="Krauth Siegel R" first="R Luise" last="Krauth-Siegel">R Luise Krauth-Siegel</name><name sortKey="Rettig, Jochen" sort="Rettig, Jochen" uniqKey="Rettig J" first="Jochen" last="Rettig">Jochen Rettig</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
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|texte= Monothiol glutaredoxin-1 is an essential iron-sulfur protein in the mitochondrion of African trypanosomes.
}}
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