Glutathionylation of trypanosomal thiol redox proteins.
Identifieur interne : 000C82 ( Main/Exploration ); précédent : 000C81; suivant : 000C83Glutathionylation of trypanosomal thiol redox proteins.
Auteurs : Johannes Melchers [Allemagne] ; Natalie Dirdjaja ; Thomas Ruppert ; R Luise Krauth-SiegelSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cystéine (composition chimique), Disulfures (composition chimique), Données de séquences moléculaires (MeSH), Glutathion (analogues et dérivés), Glutathion (composition chimique), Insuline (composition chimique), Oxydoréduction (MeSH), Similitude de séquences d'acides aminés (MeSH), Spectrométrie de masse ESI (MeSH), Spectrométrie de masse MALDI (MeSH), Spermidine (analogues et dérivés), Spermidine (composition chimique), Séquence d'acides aminés (MeSH), Thiols (composition chimique), Trypanosoma (MeSH).
- MESH :
- analogues et dérivés : Glutathion, Spermidine.
- composition chimique : Cystéine, Disulfures, Glutathion, Insuline, Spermidine, Thiols.
- Animaux, Données de séquences moléculaires, Oxydoréduction, Similitude de séquences d'acides aminés, Spectrométrie de masse ESI, Spectrométrie de masse MALDI, Séquence d'acides aminés, Trypanosoma.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Cysteine (chemistry), Disulfides (chemistry), Glutathione (analogs & derivatives), Glutathione (chemistry), Insulin (chemistry), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Sequence Homology, Amino Acid (MeSH), Spectrometry, Mass, Electrospray Ionization (MeSH), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH), Spermidine (analogs & derivatives), Spermidine (chemistry), Sulfhydryl Compounds (chemistry), Trypanosoma (MeSH).
- MESH :
- chemical , analogs & derivatives : Glutathione, Spermidine.
- chemical , chemistry : Cysteine, Disulfides, Glutathione, Insulin, Spermidine, Sulfhydryl Compounds.
- Amino Acid Sequence, Animals, Molecular Sequence Data, Oxidation-Reduction, Sequence Homology, Amino Acid, Spectrometry, Mass, Electrospray Ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Trypanosoma.
Abstract
Trypanosomatids, the causative agents of several tropical diseases, lack glutathione reductase and thioredoxin reductase but have a trypanothione reductase instead. The main low molecular weight thiols are trypanothione (N(1),N(8)-bis-(glutathionyl)spermidine) and glutathionyl-spermidine, but the parasites also contain free glutathione. To elucidate whether trypanosomes employ S-thiolation for regulatory or protection purposes, six recombinant parasite thiol redox proteins were studied by ESI-MS and MALDI-TOF-MS for their ability to form mixed disulfides with glutathione or glutathionylspermidine. Trypanosoma brucei mono-Cys-glutaredoxin 1 is specifically thiolated at Cys(181). Thiolation of this residue induced formation of an intramolecular disulfide bridge with the putative active site Cys(104). This contrasts with mono-Cys-glutaredoxins from other sources that have been reported to be glutathionylated at the active site cysteine. Both disulfide forms of the T. brucei protein were reduced by tryparedoxin and trypanothione, whereas glutathione cleaved only the protein disulfide. In the glutathione peroxidase-type tryparedoxin peroxidase III of T. brucei, either Cys(47) or Cys(95) became glutathionylated but not both residues in the same protein molecule. T. brucei thioredoxin contains a third cysteine (Cys(68)) in addition to the redox active dithiol/disulfide. Treatment of the reduced protein with GSSG caused glutathionylation of Cys(68), which did not affect its capacity to catalyze reduction of insulin disulfide. Reduced T. brucei tryparedoxin possesses only the redox active Cys(32)-Cys(35) couple, which upon reaction with GSSG formed a disulfide. Also glyoxalase II and Trypanosoma cruzi trypanothione reductase were not sensitive to thiolation at physiological GSSG concentrations.
DOI: 10.1074/jbc.M608140200
PubMed: 17242409
Affiliations:
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Le document en format XML
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last="Melchers">Johannes Melchers</name><affiliation wicri:level="3"><nlm:affiliation>Biochemie-Zentrum, Universität, Heidelberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Biochemie-Zentrum, Universität, 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="Dirdjaja, Natalie" sort="Dirdjaja, Natalie" uniqKey="Dirdjaja N" first="Natalie" last="Dirdjaja">Natalie Dirdjaja</name></author><author><name sortKey="Ruppert, Thomas" sort="Ruppert, Thomas" uniqKey="Ruppert T" first="Thomas" last="Ruppert">Thomas Ruppert</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="2007" type="published">2007</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>Cysteine (chemistry)</term><term>Disulfides (chemistry)</term><term>Glutathione (analogs & derivatives)</term><term>Glutathione (chemistry)</term><term>Insulin (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Spectrometry, Mass, Electrospray Ionization (MeSH)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH)</term><term>Spermidine (analogs & derivatives)</term><term>Spermidine (chemistry)</term><term>Sulfhydryl Compounds (chemistry)</term><term>Trypanosoma (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cystéine (composition chimique)</term><term>Disulfures (composition chimique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutathion (analogues et dérivés)</term><term>Glutathion (composition chimique)</term><term>Insuline (composition chimique)</term><term>Oxydoréduction (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Spectrométrie de masse ESI (MeSH)</term><term>Spectrométrie de masse MALDI (MeSH)</term><term>Spermidine (analogues et dérivés)</term><term>Spermidine (composition chimique)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiols (composition chimique)</term><term>Trypanosoma (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Glutathione</term><term>Spermidine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Disulfides</term><term>Glutathione</term><term>Insulin</term><term>Spermidine</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Glutathion</term><term>Spermidine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Disulfures</term><term>Glutathion</term><term>Insuline</term><term>Spermidine</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Sequence Homology, Amino Acid</term><term>Spectrometry, Mass, Electrospray Ionization</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term><term>Trypanosoma</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Données de séquences moléculaires</term><term>Oxydoréduction</term><term>Similitude de séquences d'acides aminés</term><term>Spectrométrie de masse ESI</term><term>Spectrométrie de masse MALDI</term><term>Séquence d'acides aminés</term><term>Trypanosoma</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Trypanosomatids, the causative agents of several tropical diseases, lack glutathione reductase and thioredoxin reductase but have a trypanothione reductase instead. The main low molecular weight thiols are trypanothione (N(1),N(8)-bis-(glutathionyl)spermidine) and glutathionyl-spermidine, but the parasites also contain free glutathione. To elucidate whether trypanosomes employ S-thiolation for regulatory or protection purposes, six recombinant parasite thiol redox proteins were studied by ESI-MS and MALDI-TOF-MS for their ability to form mixed disulfides with glutathione or glutathionylspermidine. Trypanosoma brucei mono-Cys-glutaredoxin 1 is specifically thiolated at Cys(181). Thiolation of this residue induced formation of an intramolecular disulfide bridge with the putative active site Cys(104). This contrasts with mono-Cys-glutaredoxins from other sources that have been reported to be glutathionylated at the active site cysteine. Both disulfide forms of the T. brucei protein were reduced by tryparedoxin and trypanothione, whereas glutathione cleaved only the protein disulfide. In the glutathione peroxidase-type tryparedoxin peroxidase III of T. brucei, either Cys(47) or Cys(95) became glutathionylated but not both residues in the same protein molecule. T. brucei thioredoxin contains a third cysteine (Cys(68)) in addition to the redox active dithiol/disulfide. Treatment of the reduced protein with GSSG caused glutathionylation of Cys(68), which did not affect its capacity to catalyze reduction of insulin disulfide. Reduced T. brucei tryparedoxin possesses only the redox active Cys(32)-Cys(35) couple, which upon reaction with GSSG formed a disulfide. Also glyoxalase II and Trypanosoma cruzi trypanothione reductase were not sensitive to thiolation at physiological GSSG concentrations.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17242409</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>02</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>282</Volume><Issue>12</Issue><PubDate><Year>2007</Year><Month>Mar</Month><Day>23</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Glutathionylation of trypanosomal thiol redox proteins.</ArticleTitle><Pagination><MedlinePgn>8678-94</MedlinePgn></Pagination><Abstract><AbstractText>Trypanosomatids, the causative agents of several tropical diseases, lack glutathione reductase and thioredoxin reductase but have a trypanothione reductase instead. The main low molecular weight thiols are trypanothione (N(1),N(8)-bis-(glutathionyl)spermidine) and glutathionyl-spermidine, but the parasites also contain free glutathione. To elucidate whether trypanosomes employ S-thiolation for regulatory or protection purposes, six recombinant parasite thiol redox proteins were studied by ESI-MS and MALDI-TOF-MS for their ability to form mixed disulfides with glutathione or glutathionylspermidine. Trypanosoma brucei mono-Cys-glutaredoxin 1 is specifically thiolated at Cys(181). Thiolation of this residue induced formation of an intramolecular disulfide bridge with the putative active site Cys(104). This contrasts with mono-Cys-glutaredoxins from other sources that have been reported to be glutathionylated at the active site cysteine. Both disulfide forms of the T. brucei protein were reduced by tryparedoxin and trypanothione, whereas glutathione cleaved only the protein disulfide. In the glutathione peroxidase-type tryparedoxin peroxidase III of T. brucei, either Cys(47) or Cys(95) became glutathionylated but not both residues in the same protein molecule. T. brucei thioredoxin contains a third cysteine (Cys(68)) in addition to the redox active dithiol/disulfide. Treatment of the reduced protein with GSSG caused glutathionylation of Cys(68), which did not affect its capacity to catalyze reduction of insulin disulfide. Reduced T. brucei tryparedoxin possesses only the redox active Cys(32)-Cys(35) couple, which upon reaction with GSSG formed a disulfide. Also glyoxalase II and Trypanosoma cruzi trypanothione reductase were not sensitive to thiolation at physiological GSSG concentrations.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Melchers</LastName><ForeName>Johannes</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Biochemie-Zentrum, Universität, Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dirdjaja</LastName><ForeName>Natalie</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Ruppert</LastName><ForeName>Thomas</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Krauth-Siegel</LastName><ForeName>R Luise</ForeName><Initials>RL</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AJ619696</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>01</Month><Day>22</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="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007328">Insulin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>33932-35-3</RegistryNumber><NameOfSubstance UI="C012333">glutathionylspermidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>96304-42-6</RegistryNumber><NameOfSubstance UI="C044809">trypanothione</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>U87FK77H25</RegistryNumber><NameOfSubstance UI="D013095">Spermidine</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="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007328" MajorTopicYN="N">Insulin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</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="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021241" MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019032" MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013095" MajorTopicYN="N">Spermidine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014345" MajorTopicYN="N">Trypanosoma</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>1</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>5</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>1</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17242409</ArticleId><ArticleId IdType="pii">M608140200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M608140200</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="Dirdjaja, Natalie" sort="Dirdjaja, Natalie" uniqKey="Dirdjaja N" first="Natalie" last="Dirdjaja">Natalie Dirdjaja</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="Ruppert, Thomas" sort="Ruppert, Thomas" uniqKey="Ruppert T" first="Thomas" last="Ruppert">Thomas Ruppert</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Melchers, Johannes" sort="Melchers, Johannes" uniqKey="Melchers J" first="Johannes" last="Melchers">Johannes Melchers</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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