The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism.
Identifieur interne : 000985 ( Main/Exploration ); précédent : 000984; suivant : 000986The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism.
Auteurs : Sevgi Ceylan [Allemagne] ; Vera Seidel ; Nicole Ziebart ; Carsten Berndt ; Natalie Dirdjaja ; R Luise Krauth-SiegelSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cytochromes c (génétique), Cytochromes c (métabolisme), Domaine catalytique (MeSH), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (analogues et dérivés), Glutathion (génétique), Glutathion (métabolisme), Membranes mitochondriales (enzymologie), Oxydoréduction (MeSH), Protéines de protozoaire (génétique), Protéines de protozoaire (métabolisme), Protéines mitochondriales (génétique), Protéines mitochondriales (métabolisme), Spermidine (analogues et dérivés), Spermidine (métabolisme), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Trypanosoma brucei brucei (enzymologie).
- MESH :
- analogues et dérivés : Glutathion, Spermidine.
- enzymologie : Membranes mitochondriales, Trypanosoma brucei brucei.
- génétique : Cytochromes c, Glutarédoxines, Glutathion, Protéines de protozoaire, Protéines mitochondriales, Thiorédoxines.
- métabolisme : Cytochromes c, Glutarédoxines, Glutathion, Protéines de protozoaire, Protéines mitochondriales, Spermidine, Thiorédoxines.
- Animaux, Domaine catalytique, Oxydoréduction.
English descriptors
- KwdEn :
- Animals (MeSH), Catalytic Domain (MeSH), Cytochromes c (genetics), Cytochromes c (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (analogs & derivatives), Glutathione (genetics), Glutathione (metabolism), Mitochondrial Membranes (enzymology), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Oxidation-Reduction (MeSH), Protozoan Proteins (genetics), Protozoan Proteins (metabolism), Spermidine (analogs & derivatives), Spermidine (metabolism), Thioredoxins (genetics), Thioredoxins (metabolism), Trypanosoma brucei brucei (enzymology).
- MESH :
- chemical , analogs & derivatives : Glutathione, Spermidine.
- chemical , genetics : Cytochromes c, Glutaredoxins, Glutathione, Mitochondrial Proteins, Protozoan Proteins, Thioredoxins.
- chemical , metabolism : Cytochromes c, Glutaredoxins, Glutathione, Mitochondrial Proteins, Protozoan Proteins, Spermidine, Thioredoxins.
- enzymology : Mitochondrial Membranes, Trypanosoma brucei brucei.
- Animals, Catalytic Domain, Oxidation-Reduction.
Abstract
Trypanosoma brucei, the causative agent of African sleeping sickness, possesses two dithiol glutaredoxins (Grx1 and Grx2). Grx1 occurs in the cytosol and catalyzes protein deglutathionylations with k(cat)/K(m)-values of up to 2 × 10(5) M(-1) S(-1). It accelerates the reduction of ribonucleotide reductase by trypanothione although less efficiently than the parasite tryparedoxin and has low insulin disulfide reductase activity. Despite its classical CPYC active site, Grx1 forms dimeric iron-sulfur complexes with GSH, glutathionylspermidine, or trypanothione as non-protein ligands. Thus, contrary to the generally accepted assumption, replacement of the Pro is not a prerequisite for cluster formation. T. brucei Grx2 shows an unusual CQFC active site, and orthologues occur exclusively in trypanosomatids. Grx2 is enriched in mitoplasts, and fractionated digitonin lysis resulted in a co-elution with cytochrome c, suggesting localization in the mitochondrial intermembrane space. Grx2 catalyzes the reduction of insulin disulfide but not of ribonucleotide reductase and exerts deglutathionylation activity 10-fold lower than that of Grx1. RNA interference against Grx2 caused a growth retardation of procyclic cells consistent with an essential role. Grx1 and Grx2 are constitutively expressed with cellular concentrations of about 2 μM and 200 nM, respectively, in both the mammalian bloodstream and insect procyclic forms. Trypanothione reduces the disulfide form of both proteins with apparent rate constants that are 3 orders of magnitude higher than those with glutathione. Grx1 and, less efficiently, also Grx2 catalyze the reduction of GSSG by trypanothione. Thus, the Grxs play exclusive roles in the trypanothione-based thiol redox metabolism of African trypanosomes.
DOI: 10.1074/jbc.M110.165860
PubMed: 20826822
PubMed Central: PMC2966136
Affiliations:
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scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cytochromes c (génétique)</term><term>Cytochromes c (métabolisme)</term><term>Domaine catalytique (MeSH)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (analogues et dérivés)</term><term>Glutathion (génétique)</term><term>Glutathion (métabolisme)</term><term>Membranes mitochondriales (enzymologie)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de protozoaire (génétique)</term><term>Protéines de protozoaire (métabolisme)</term><term>Protéines mitochondriales (génétique)</term><term>Protéines mitochondriales (métabolisme)</term><term>Spermidine (analogues et dérivés)</term><term>Spermidine (métabolisme)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term><term>Trypanosoma brucei brucei (enzymologie)</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="genetics" xml:lang="en"><term>Cytochromes c</term><term>Glutaredoxins</term><term>Glutathione</term><term>Mitochondrial Proteins</term><term>Protozoan Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytochromes c</term><term>Glutaredoxins</term><term>Glutathione</term><term>Mitochondrial Proteins</term><term>Protozoan Proteins</term><term>Spermidine</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Glutathion</term><term>Spermidine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Membranes mitochondriales</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Mitochondrial Membranes</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cytochromes c</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines de protozoaire</term><term>Protéines mitochondriales</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytochromes c</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines de protozoaire</term><term>Protéines mitochondriales</term><term>Spermidine</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Catalytic Domain</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Domaine catalytique</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Trypanosoma brucei, the causative agent of African sleeping sickness, possesses two dithiol glutaredoxins (Grx1 and Grx2). Grx1 occurs in the cytosol and catalyzes protein deglutathionylations with k(cat)/K(m)-values of up to 2 × 10(5) M(-1) S(-1). It accelerates the reduction of ribonucleotide reductase by trypanothione although less efficiently than the parasite tryparedoxin and has low insulin disulfide reductase activity. Despite its classical CPYC active site, Grx1 forms dimeric iron-sulfur complexes with GSH, glutathionylspermidine, or trypanothione as non-protein ligands. Thus, contrary to the generally accepted assumption, replacement of the Pro is not a prerequisite for cluster formation. T. brucei Grx2 shows an unusual CQFC active site, and orthologues occur exclusively in trypanosomatids. Grx2 is enriched in mitoplasts, and fractionated digitonin lysis resulted in a co-elution with cytochrome c, suggesting localization in the mitochondrial intermembrane space. Grx2 catalyzes the reduction of insulin disulfide but not of ribonucleotide reductase and exerts deglutathionylation activity 10-fold lower than that of Grx1. RNA interference against Grx2 caused a growth retardation of procyclic cells consistent with an essential role. Grx1 and Grx2 are constitutively expressed with cellular concentrations of about 2 μM and 200 nM, respectively, in both the mammalian bloodstream and insect procyclic forms. Trypanothione reduces the disulfide form of both proteins with apparent rate constants that are 3 orders of magnitude higher than those with glutathione. Grx1 and, less efficiently, also Grx2 catalyze the reduction of GSSG by trypanothione. Thus, the Grxs play exclusive roles in the trypanothione-based thiol redox metabolism of African trypanosomes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20826822</PMID><DateCompleted><Year>2010</Year><Month>11</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>285</Volume><Issue>45</Issue><PubDate><Year>2010</Year><Month>Nov</Month><Day>05</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism.</ArticleTitle><Pagination><MedlinePgn>35224-37</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M110.165860</ELocationID><Abstract><AbstractText>Trypanosoma brucei, the causative agent of African sleeping sickness, possesses two dithiol glutaredoxins (Grx1 and Grx2). Grx1 occurs in the cytosol and catalyzes protein deglutathionylations with k(cat)/K(m)-values of up to 2 × 10(5) M(-1) S(-1). It accelerates the reduction of ribonucleotide reductase by trypanothione although less efficiently than the parasite tryparedoxin and has low insulin disulfide reductase activity. Despite its classical CPYC active site, Grx1 forms dimeric iron-sulfur complexes with GSH, glutathionylspermidine, or trypanothione as non-protein ligands. Thus, contrary to the generally accepted assumption, replacement of the Pro is not a prerequisite for cluster formation. T. brucei Grx2 shows an unusual CQFC active site, and orthologues occur exclusively in trypanosomatids. Grx2 is enriched in mitoplasts, and fractionated digitonin lysis resulted in a co-elution with cytochrome c, suggesting localization in the mitochondrial intermembrane space. Grx2 catalyzes the reduction of insulin disulfide but not of ribonucleotide reductase and exerts deglutathionylation activity 10-fold lower than that of Grx1. RNA interference against Grx2 caused a growth retardation of procyclic cells consistent with an essential role. Grx1 and Grx2 are constitutively expressed with cellular concentrations of about 2 μM and 200 nM, respectively, in both the mammalian bloodstream and insect procyclic forms. Trypanothione reduces the disulfide form of both proteins with apparent rate constants that are 3 orders of magnitude higher than those with glutathione. Grx1 and, less efficiently, also Grx2 catalyze the reduction of GSSG by trypanothione. Thus, the Grxs play exclusive roles in the trypanothione-based thiol redox metabolism of African trypanosomes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ceylan</LastName><ForeName>Sevgi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Seidel</LastName><ForeName>Vera</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Ziebart</LastName><ForeName>Nicole</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Dirdjaja</LastName><ForeName>Natalie</ForeName><Initials>N</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>2010</Year><Month>09</Month><Day>08</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="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015800">Protozoan Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C114110">tryparedoxin</NameOfSubstance></Chemical><Chemical><RegistryNumber>33932-35-3</RegistryNumber><NameOfSubstance UI="C012333">glutathionylspermidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-43-6</RegistryNumber><NameOfSubstance UI="D045304">Cytochromes c</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>U87FK77H25</RegistryNumber><NameOfSubstance UI="D013095">Spermidine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045304" MajorTopicYN="N">Cytochromes c</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051336" MajorTopicYN="N">Mitochondrial Membranes</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024101" MajorTopicYN="N">Mitochondrial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015800" MajorTopicYN="N">Protozoan Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013095" MajorTopicYN="N">Spermidine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><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="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014346" MajorTopicYN="N">Trypanosoma brucei brucei</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>12</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20826822</ArticleId><ArticleId 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