Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes.
Identifieur interne : 000737 ( Main/Exploration ); précédent : 000736; suivant : 000738Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes.
Auteurs : Marcelo A. Comini [Uruguay] ; R Luise Krauth-Siegel ; Massimo BellandaSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (physiologie), Glutathion (analogues et dérivés), Glutathion (métabolisme), Humains (MeSH), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Protéines de protozoaire (composition chimique), Protéines de protozoaire (physiologie), Spermidine (analogues et dérivés), Spermidine (métabolisme), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Trypanosoma (enzymologie), Trypanosomiase (parasitologie).
- MESH :
- analogues et dérivés : Glutathion, Spermidine.
- composition chimique : Glutarédoxines, Protéines de protozoaire.
- enzymologie : Trypanosoma.
- métabolisme : Glutathion, Spermidine.
- parasitologie : Trypanosomiase.
- physiologie : Glutarédoxines, Protéines de protozoaire.
- Animaux, Conformation des protéines, Données de séquences moléculaires, Humains, Modèles moléculaires, Oxydoréduction, Séquence conservée, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Conserved Sequence (MeSH), Glutaredoxins (chemistry), Glutaredoxins (physiology), Glutathione (analogs & derivatives), Glutathione (metabolism), Humans (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Protein Conformation (MeSH), Protozoan Proteins (chemistry), Protozoan Proteins (physiology), Spermidine (analogs & derivatives), Spermidine (metabolism), Trypanosoma (enzymology), Trypanosomiasis (parasitology).
- MESH :
- chemical , analogs & derivatives : Glutathione, Spermidine.
- chemical , chemistry : Glutaredoxins, Protozoan Proteins.
- chemical , metabolism : Glutathione, Spermidine.
- chemical , physiology : Glutaredoxins, Protozoan Proteins.
- enzymology : Trypanosoma.
- parasitology : Trypanosomiasis.
- Amino Acid Sequence, Animals, Conserved Sequence, Humans, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation.
Abstract
SIGNIFICANCE
Glutaredoxins are ubiquitous small thiol proteins of the thioredoxin-fold superfamily. Two major groups are distinguished based on their active sites: the dithiol (2-C-Grxs) and the monothiol (1-C-Grxs) glutaredoxins with a CXXC and a CXXS active site motif, respectively. Glutaredoxins are involved in cellular redox and/or iron sulfur metabolism. Usually their functions are closely linked to the glutathione system. Trypanosomatids, the causative agents of several tropical diseases, rely on trypanothione as principal low molecular mass thiol, and their glutaredoxins readily react with the unique bis(glutathionyl) spermidine conjugate.
RECENT ADVANCES
Two 2-C-Grxs and three 1-C-Grxs have been identified in pathogenic trypanosomatids. The 2-C-Grxs catalyze the reduction of glutathione disulfide by trypanothione and display reductase activity towards protein disulfides, as well as protein-glutathione mixed disulfides. In vitro, all three 1-C-Grxs as well as the cytosolic 2-C-Grx of Trypanosoma brucei can complex an iron-sulfur cluster. Recently the structure of the 1-C-Grx1 has been solved by NMR spectroscopy. The structure is very similar to those of other 1-C-Grxs, with some differences in the loop containing the conserved cis-Pro and the surface charge distribution.
CRITICAL ISSUES
Although four of the five trypanosomal glutaredoxins proved to coordinate an iron-sulfur cluster in vitro, the physiological role of the mitochondrial and cytosolic proteins, respectively, has only started to be unraveled.
FUTURE DIRECTIONS
The use of trypanothione by the glutaredoxins has established a novel role for this parasite-specific dithiol. Future work should reveal if these differences can be exploited for the development of novel antiparasitic drugs.
DOI: 10.1089/ars.2012.4932
PubMed: 22978520
PubMed Central: PMC3739957
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Comini</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Montevideo, Uruguay. mcomini@pasteur.edu.uy</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></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><author><name sortKey="Bellanda, Massimo" sort="Bellanda, Massimo" uniqKey="Bellanda M" first="Massimo" last="Bellanda">Massimo Bellanda</name></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2013" type="published">2013</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>Conserved Sequence (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (physiology)</term><term>Glutathione (analogs & derivatives)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protozoan Proteins (chemistry)</term><term>Protozoan Proteins (physiology)</term><term>Spermidine (analogs & derivatives)</term><term>Spermidine (metabolism)</term><term>Trypanosoma (enzymology)</term><term>Trypanosomiasis (parasitology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (physiologie)</term><term>Glutathion (analogues et dérivés)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de protozoaire (composition chimique)</term><term>Protéines de protozoaire (physiologie)</term><term>Spermidine (analogues et dérivés)</term><term>Spermidine (métabolisme)</term><term>Séquence conservée (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Trypanosoma (enzymologie)</term><term>Trypanosomiase (parasitologie)</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>Glutaredoxins</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Spermidine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Glutaredoxins</term><term>Protozoan Proteins</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>Glutarédoxines</term><term>Protéines de protozoaire</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Trypanosoma</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Trypanosoma</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Spermidine</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Trypanosomiase</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Trypanosomiasis</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines de protozoaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Conserved Sequence</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>SIGNIFICANCE</b></p><p>Glutaredoxins are ubiquitous small thiol proteins of the thioredoxin-fold superfamily. Two major groups are distinguished based on their active sites: the dithiol (2-C-Grxs) and the monothiol (1-C-Grxs) glutaredoxins with a CXXC and a CXXS active site motif, respectively. Glutaredoxins are involved in cellular redox and/or iron sulfur metabolism. Usually their functions are closely linked to the glutathione system. Trypanosomatids, the causative agents of several tropical diseases, rely on trypanothione as principal low molecular mass thiol, and their glutaredoxins readily react with the unique bis(glutathionyl) spermidine conjugate.</p></div><div type="abstract" xml:lang="en"><p><b>RECENT ADVANCES</b></p><p>Two 2-C-Grxs and three 1-C-Grxs have been identified in pathogenic trypanosomatids. The 2-C-Grxs catalyze the reduction of glutathione disulfide by trypanothione and display reductase activity towards protein disulfides, as well as protein-glutathione mixed disulfides. In vitro, all three 1-C-Grxs as well as the cytosolic 2-C-Grx of Trypanosoma brucei can complex an iron-sulfur cluster. Recently the structure of the 1-C-Grx1 has been solved by NMR spectroscopy. The structure is very similar to those of other 1-C-Grxs, with some differences in the loop containing the conserved cis-Pro and the surface charge distribution.</p></div><div type="abstract" xml:lang="en"><p><b>CRITICAL ISSUES</b></p><p>Although four of the five trypanosomal glutaredoxins proved to coordinate an iron-sulfur cluster in vitro, the physiological role of the mitochondrial and cytosolic proteins, respectively, has only started to be unraveled.</p></div><div type="abstract" xml:lang="en"><p><b>FUTURE DIRECTIONS</b></p><p>The use of trypanothione by the glutaredoxins has established a novel role for this parasite-specific dithiol. Future work should reveal if these differences can be exploited for the development of novel antiparasitic drugs.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22978520</PMID><DateCompleted><Year>2014</Year><Month>02</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>19</Volume><Issue>7</Issue><PubDate><Year>2013</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes.</ArticleTitle><Pagination><MedlinePgn>708-22</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2012.4932</ELocationID><Abstract><AbstractText Label="SIGNIFICANCE" NlmCategory="CONCLUSIONS">Glutaredoxins are ubiquitous small thiol proteins of the thioredoxin-fold superfamily. Two major groups are distinguished based on their active sites: the dithiol (2-C-Grxs) and the monothiol (1-C-Grxs) glutaredoxins with a CXXC and a CXXS active site motif, respectively. Glutaredoxins are involved in cellular redox and/or iron sulfur metabolism. Usually their functions are closely linked to the glutathione system. Trypanosomatids, the causative agents of several tropical diseases, rely on trypanothione as principal low molecular mass thiol, and their glutaredoxins readily react with the unique bis(glutathionyl) spermidine conjugate.</AbstractText><AbstractText Label="RECENT ADVANCES" NlmCategory="BACKGROUND">Two 2-C-Grxs and three 1-C-Grxs have been identified in pathogenic trypanosomatids. The 2-C-Grxs catalyze the reduction of glutathione disulfide by trypanothione and display reductase activity towards protein disulfides, as well as protein-glutathione mixed disulfides. In vitro, all three 1-C-Grxs as well as the cytosolic 2-C-Grx of Trypanosoma brucei can complex an iron-sulfur cluster. Recently the structure of the 1-C-Grx1 has been solved by NMR spectroscopy. The structure is very similar to those of other 1-C-Grxs, with some differences in the loop containing the conserved cis-Pro and the surface charge distribution.</AbstractText><AbstractText Label="CRITICAL ISSUES" NlmCategory="RESULTS">Although four of the five trypanosomal glutaredoxins proved to coordinate an iron-sulfur cluster in vitro, the physiological role of the mitochondrial and cytosolic proteins, respectively, has only started to be unraveled.</AbstractText><AbstractText Label="FUTURE DIRECTIONS" NlmCategory="CONCLUSIONS">The use of trypanothione by the glutaredoxins has established a novel role for this parasite-specific dithiol. Future work should reveal if these differences can be exploited for the development of novel antiparasitic drugs.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Montevideo, Uruguay. mcomini@pasteur.edu.uy</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Krauth-Siegel</LastName><ForeName>R Luise</ForeName><Initials>RL</Initials></Author><Author ValidYN="Y"><LastName>Bellanda</LastName><ForeName>Massimo</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>10</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015800">Protozoan Proteins</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="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, 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