Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1.
Identifieur interne : 000C19 ( Main/Exploration ); précédent : 000C18; suivant : 000C20Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1.
Auteurs : Michael Filser [Allemagne] ; Marcelo A. Comini ; Maria M. Molina-Navarro ; Natalie Dirdjaja ; Enrique Herrero ; R Luise Krauth-SiegelSource :
- Biological chemistry [ 1431-6730 ] ; 2008.
Descripteurs français
- KwdFr :
- ADN des protozoaires (génétique), ADN des protozoaires (métabolisme), Animaux (MeSH), Chromatographie sur gel (MeSH), Clonage moléculaire (MeSH), Codon (génétique), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Fractions subcellulaires (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Insuline (métabolisme), Mitochondries (enzymologie), Mitochondries (métabolisme), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Protéines recombinantes (biosynthèse), Protéines recombinantes (génétique), Réducteurs (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Séquence d'acides aminés (MeSH), Technique de Western (MeSH), Test de complémentation (MeSH), Thiols (métabolisme), Trypanosoma brucei brucei (croissance et développement), Trypanosoma brucei brucei (génétique), Trypanosoma brucei brucei (métabolisme), Éthanol (analogues et dérivés), Éthanol (métabolisme).
- MESH :
- analogues et dérivés : Éthanol.
- biosynthèse : Protéines recombinantes.
- composition chimique : Glutarédoxines.
- croissance et développement : Trypanosoma brucei brucei.
- enzymologie : Mitochondries.
- génétique : ADN des protozoaires, Codon, Glutarédoxines, Protéines recombinantes, Saccharomyces cerevisiae, Trypanosoma brucei brucei.
- métabolisme : ADN des protozoaires, Disulfures, Fractions subcellulaires, Glutarédoxines, Insuline, Mitochondries, Oxidoreductases, Réducteurs, Saccharomyces cerevisiae, Thiols, Trypanosoma brucei brucei, Éthanol.
- Animaux, Chromatographie sur gel, Clonage moléculaire, Données de séquences moléculaires, Oxydoréduction, Séquence d'acides aminés, Technique de Western, Test de complémentation.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Blotting, Western (MeSH), Chromatography, Gel (MeSH), Cloning, Molecular (MeSH), Codon (genetics), DNA, Protozoan (genetics), DNA, Protozoan (metabolism), Disulfides (metabolism), Ethanol (analogs & derivatives), Ethanol (metabolism), Genetic Complementation Test (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Insulin (metabolism), Mitochondria (enzymology), Mitochondria (metabolism), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Recombinant Proteins (biosynthesis), Recombinant Proteins (genetics), Reducing Agents (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Subcellular Fractions (metabolism), Sulfhydryl Compounds (metabolism), Trypanosoma brucei brucei (genetics), Trypanosoma brucei brucei (growth & development), Trypanosoma brucei brucei (metabolism).
- MESH :
- chemical , analogs & derivatives : Ethanol.
- chemical , biosynthesis : Recombinant Proteins.
- chemical , chemistry : Glutaredoxins.
- chemical , genetics : Codon, DNA, Protozoan, Glutaredoxins, Recombinant Proteins.
- chemical , metabolism : DNA, Protozoan, Disulfides, Ethanol, Glutaredoxins, Insulin, Oxidoreductases, Reducing Agents, Sulfhydryl Compounds.
- enzymology : Mitochondria.
- genetics : Saccharomyces cerevisiae, Trypanosoma brucei brucei.
- growth & development : Trypanosoma brucei brucei.
- metabolism : Mitochondria, Saccharomyces cerevisiae, Subcellular Fractions, Trypanosoma brucei brucei.
- Amino Acid Sequence, Animals, Blotting, Western, Chromatography, Gel, Cloning, Molecular, Genetic Complementation Test, Molecular Sequence Data, Oxidation-Reduction.
Abstract
African trypanosomes encode three monothiol glutaredoxins (1-C-Grx1 to 3). 1-C-Grx1 has a putative CAYS active site and Cys181 as single additional cysteine. The recombinant protein forms non-covalent homodimers. As observed for other monothiol glutaredoxins, Trypanosoma brucei 1-C-Grx1 was not active in the glutaredoxin assay with hydroxyethyl disulfide and glutathione nor catalyzed the reduction of insulin disulfide. In addition, it lacked peroxidase activity and did not catalyze protein (de)glutathionylation. Upon oxidation, 1-C-Grx1 forms an intramolecular disulfide bridge and, to a minor degree, covalent dimers. Both disulfide forms are reduced by the parasite trypanothione/tryparedoxin system. 1-C-Grx1 shows mitochondrial localization. The total cellular concentration is at least 5 microm. Thus, 1-C-Grx1 is an abundant protein especially in the rudimentary organelle of the mammalian form of the parasite. Expression of 1-C-Grx1 in Grx5-deficient yeast cells with its authentic presequence targeted the protein to the mitochondria and partially restored the growth phenotype and aconitase activity of the mutant, and conferred resistance against hydroperoxides and diamide. The parasite Grx2 and 3 failed to substitute for Grx5. This is surprising because even bacterial and plant 1-Cys-glutaredoxins efficiently revert the defects, and may be due to the lack of two basic residues conserved in all but the trypanosomatid proteins.
DOI: 10.1515/BC.2007.147
PubMed: 18095866
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Comini</name></author><author><name sortKey="Molina Navarro, Maria M" sort="Molina Navarro, Maria M" uniqKey="Molina Navarro M" first="Maria M" last="Molina-Navarro">Maria M. Molina-Navarro</name></author><author><name sortKey="Dirdjaja, Natalie" sort="Dirdjaja, Natalie" uniqKey="Dirdjaja N" first="Natalie" last="Dirdjaja">Natalie Dirdjaja</name></author><author><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</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:18095866</idno><idno type="pmid">18095866</idno><idno type="doi">10.1515/BC.2007.147</idno><idno type="wicri:Area/Main/Corpus">000C26</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C26</idno><idno type="wicri:Area/Main/Curation">000C26</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C26</idno><idno type="wicri:Area/Main/Exploration">000C26</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1.</title><author><name sortKey="Filser, Michael" sort="Filser, Michael" uniqKey="Filser M" first="Michael" last="Filser">Michael Filser</name><affiliation wicri:level="3"><nlm:affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 504, D-69120 Heidelberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Biochemie-Zentrum der Universität Heidelberg, 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="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. 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Molina-Navarro</name></author><author><name sortKey="Dirdjaja, Natalie" sort="Dirdjaja, Natalie" uniqKey="Dirdjaja N" first="Natalie" last="Dirdjaja">Natalie Dirdjaja</name></author><author><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</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">Biological chemistry</title><idno type="ISSN">1431-6730</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Blotting, Western (MeSH)</term><term>Chromatography, Gel (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Codon (genetics)</term><term>DNA, Protozoan (genetics)</term><term>DNA, Protozoan (metabolism)</term><term>Disulfides (metabolism)</term><term>Ethanol (analogs & derivatives)</term><term>Ethanol (metabolism)</term><term>Genetic Complementation Test (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Insulin (metabolism)</term><term>Mitochondria (enzymology)</term><term>Mitochondria (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (genetics)</term><term>Reducing Agents (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Subcellular Fractions (metabolism)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Trypanosoma brucei brucei (genetics)</term><term>Trypanosoma brucei brucei (growth & development)</term><term>Trypanosoma brucei brucei (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN des protozoaires (génétique)</term><term>ADN des protozoaires (métabolisme)</term><term>Animaux (MeSH)</term><term>Chromatographie sur gel (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Codon (génétique)</term><term>Disulfures (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Fractions subcellulaires (métabolisme)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Insuline (métabolisme)</term><term>Mitochondries (enzymologie)</term><term>Mitochondries (métabolisme)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (génétique)</term><term>Réducteurs (métabolisme)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Technique de Western (MeSH)</term><term>Test de complémentation (MeSH)</term><term>Thiols (métabolisme)</term><term>Trypanosoma brucei brucei (croissance et développement)</term><term>Trypanosoma brucei brucei (génétique)</term><term>Trypanosoma brucei brucei (métabolisme)</term><term>Éthanol (analogues et dérivés)</term><term>Éthanol (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Ethanol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Codon</term><term>DNA, Protozoan</term><term>Glutaredoxins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA, Protozoan</term><term>Disulfides</term><term>Ethanol</term><term>Glutaredoxins</term><term>Insulin</term><term>Oxidoreductases</term><term>Reducing Agents</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Éthanol</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Mitochondries</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN des protozoaires</term><term>Codon</term><term>Glutarédoxines</term><term>Protéines recombinantes</term><term>Saccharomyces cerevisiae</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>Saccharomyces cerevisiae</term><term>Subcellular Fractions</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN des protozoaires</term><term>Disulfures</term><term>Fractions subcellulaires</term><term>Glutarédoxines</term><term>Insuline</term><term>Mitochondries</term><term>Oxidoreductases</term><term>Réducteurs</term><term>Saccharomyces cerevisiae</term><term>Thiols</term><term>Trypanosoma brucei brucei</term><term>Éthanol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Blotting, Western</term><term>Chromatography, Gel</term><term>Cloning, Molecular</term><term>Genetic Complementation Test</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chromatographie sur gel</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Oxydoréduction</term><term>Séquence d'acides aminés</term><term>Technique de Western</term><term>Test de complémentation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">African trypanosomes encode three monothiol glutaredoxins (1-C-Grx1 to 3). 1-C-Grx1 has a putative CAYS active site and Cys181 as single additional cysteine. The recombinant protein forms non-covalent homodimers. As observed for other monothiol glutaredoxins, Trypanosoma brucei 1-C-Grx1 was not active in the glutaredoxin assay with hydroxyethyl disulfide and glutathione nor catalyzed the reduction of insulin disulfide. In addition, it lacked peroxidase activity and did not catalyze protein (de)glutathionylation. Upon oxidation, 1-C-Grx1 forms an intramolecular disulfide bridge and, to a minor degree, covalent dimers. Both disulfide forms are reduced by the parasite trypanothione/tryparedoxin system. 1-C-Grx1 shows mitochondrial localization. The total cellular concentration is at least 5 microm. Thus, 1-C-Grx1 is an abundant protein especially in the rudimentary organelle of the mammalian form of the parasite. Expression of 1-C-Grx1 in Grx5-deficient yeast cells with its authentic presequence targeted the protein to the mitochondria and partially restored the growth phenotype and aconitase activity of the mutant, and conferred resistance against hydroperoxides and diamide. The parasite Grx2 and 3 failed to substitute for Grx5. This is surprising because even bacterial and plant 1-Cys-glutaredoxins efficiently revert the defects, and may be due to the lack of two basic residues conserved in all but the trypanosomatid proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18095866</PMID><DateCompleted><Year>2008</Year><Month>02</Month><Day>20</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1431-6730</ISSN><JournalIssue CitedMedium="Print"><Volume>389</Volume><Issue>1</Issue><PubDate><Year>2008</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Biological chemistry</Title><ISOAbbreviation>Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1.</ArticleTitle><Pagination><MedlinePgn>21-32</MedlinePgn></Pagination><Abstract><AbstractText>African trypanosomes encode three monothiol glutaredoxins (1-C-Grx1 to 3). 1-C-Grx1 has a putative CAYS active site and Cys181 as single additional cysteine. The recombinant protein forms non-covalent homodimers. As observed for other monothiol glutaredoxins, Trypanosoma brucei 1-C-Grx1 was not active in the glutaredoxin assay with hydroxyethyl disulfide and glutathione nor catalyzed the reduction of insulin disulfide. In addition, it lacked peroxidase activity and did not catalyze protein (de)glutathionylation. Upon oxidation, 1-C-Grx1 forms an intramolecular disulfide bridge and, to a minor degree, covalent dimers. Both disulfide forms are reduced by the parasite trypanothione/tryparedoxin system. 1-C-Grx1 shows mitochondrial localization. The total cellular concentration is at least 5 microm. Thus, 1-C-Grx1 is an abundant protein especially in the rudimentary organelle of the mammalian form of the parasite. Expression of 1-C-Grx1 in Grx5-deficient yeast cells with its authentic presequence targeted the protein to the mitochondria and partially restored the growth phenotype and aconitase activity of the mutant, and conferred resistance against hydroperoxides and diamide. The parasite Grx2 and 3 failed to substitute for Grx5. This is surprising because even bacterial and plant 1-Cys-glutaredoxins efficiently revert the defects, and may be due to the lack of two basic residues conserved in all but the trypanosomatid proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Filser</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 504, D-69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Molina-Navarro</LastName><ForeName>Maria M</ForeName><Initials>MM</Initials></Author><Author ValidYN="Y"><LastName>Dirdjaja</LastName><ForeName>Natalie</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</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></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Biol Chem</MedlineTA><NlmUniqueID>9700112</NlmUniqueID><ISSNLinking>1431-6730</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003062">Codon</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016054">DNA, Protozoan</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007328">Insulin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019163">Reducing Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>3K9958V90M</RegistryNumber><NameOfSubstance UI="D000431">Ethanol</NameOfSubstance></Chemical><Chemical><RegistryNumber>45543L74BS</RegistryNumber><NameOfSubstance UI="C031319">2-hydroxyethyl disulfide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003062" MajorTopicYN="N">Codon</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016054" MajorTopicYN="N">DNA, Protozoan</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000431" MajorTopicYN="N">Ethanol</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007328" MajorTopicYN="N">Insulin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><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="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019163" MajorTopicYN="N">Reducing Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013347" MajorTopicYN="N">Subcellular Fractions</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014346" MajorTopicYN="N">Trypanosoma brucei brucei</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>12</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>2</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>12</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18095866</ArticleId><ArticleId IdType="doi">10.1515/BC.2007.147</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="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><name sortKey="Dirdjaja, Natalie" sort="Dirdjaja, Natalie" uniqKey="Dirdjaja N" first="Natalie" last="Dirdjaja">Natalie Dirdjaja</name><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</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="Molina Navarro, Maria M" sort="Molina Navarro, Maria M" uniqKey="Molina Navarro M" first="Maria M" last="Molina-Navarro">Maria M. Molina-Navarro</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Filser, Michael" sort="Filser, Michael" uniqKey="Filser M" first="Michael" last="Filser">Michael Filser</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Bois
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|texte= Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1.
}}
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