Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasites.
Identifieur interne : 000152 ( Main/Exploration ); précédent : 000151; suivant : 000153Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasites.
Auteurs : Bruno Manta [Uruguay] ; Matías N. Möller ; Mariana Bonilla [Uruguay] ; Matías Deambrosi [Uruguay] ; Karin Grunberg [Uruguay] ; Massimo Bellanda [Italie] ; Marcelo A. Comini [Uruguay] ; Gerardo Ferrer-Sueta [Uruguay]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Glutarédoxines.
- métabolisme : Glutarédoxines, Thiols, Trypanosoma.
- Animaux, Cinétique, Domaine catalytique, Humains, Oxydoréduction, Évolution biologique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Glutaredoxins.
- chemical , metabolism : Glutaredoxins, Sulfhydryl Compounds.
- metabolism : Trypanosoma.
- Animals, Biological Evolution, Catalytic Domain, Humans, Kinetics, Oxidation-Reduction.
Abstract
Trypanosomes are flagellated protozoan parasites (kinetoplastids) that have a unique redox metabolism based on the small dithiol trypanothione (T(SH)2). Although GSH may still play a biological role in trypanosomatid parasites beyond being a building block of T(SH)2, most of its functions are replaced by T(SH)2 in these organisms. Consequently, trypanosomes have several enzymes adapted to using T(SH)2 instead of GSH, including the glutaredoxins (Grxs). However, the mechanistic basis of Grx specificity for T(SH)2 is unknown. Here, we combined fast-kinetic and biophysical approaches, including NMR, MS, and fluorescent tagging, to study the redox function of Grx1, the only cytosolic redox-active Grx in trypanosomes. We observed that Grx1 reduces GSH-containing disulfides (including oxidized trypanothione) in very fast reactions (k > 5 × 105 m-1 s-1). We also noted that disulfides without a GSH are much slower oxidants, suggesting a strongly selective binding of the GSH molecule. Not surprisingly, oxidized Grx1 was also reduced very fast by T(SH)2 (4.8 × 106 m-1 s-1); however, GSH-mediated reduction was extremely slow (39 m-1 s-1). This kinetic selectivity in the reduction step of the catalytic cycle suggests that Grx1 uses preferentially a dithiol mechanism, forming a disulfide on the active site during the oxidative half of the catalytic cycle and then being rapidly reduced by T(SH)2 in the reductive half. Thus, the reduction of glutathionylated substrates avoids GSSG accumulation in an organism lacking GSH reductase. These findings suggest that Grx1 has played an important adaptive role during the rewiring of the thiol-redox metabolism of kinetoplastids.
DOI: 10.1074/jbc.RA118.006366
PubMed: 30593501
PubMed Central: PMC6398122
Affiliations:
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Comini</name><affiliation wicri:level="1"><nlm:affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation></author><author><name sortKey="Ferrer Sueta, Gerardo" sort="Ferrer Sueta, Gerardo" uniqKey="Ferrer Sueta G" first="Gerardo" last="Ferrer-Sueta">Gerardo Ferrer-Sueta</name><affiliation wicri:level="1"><nlm:affiliation>the Laboratorio de Fisicoquímica Biológica and gferrer@fcien.edu.uy.</nlm:affiliation><country wicri:rule="url">Uruguay</country></affiliation><affiliation><nlm:affiliation>the Center for Free Radical and Biomedical Research, Universidad de la República, Montevideo, Uruguay, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:30593501</idno><idno type="pmid">30593501</idno><idno type="doi">10.1074/jbc.RA118.006366</idno><idno type="pmc">PMC6398122</idno><idno type="wicri:Area/Main/Corpus">000180</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000180</idno><idno type="wicri:Area/Main/Curation">000180</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000180</idno><idno type="wicri:Area/Main/Exploration">000180</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasites.</title><author><name sortKey="Manta, Bruno" sort="Manta, Bruno" uniqKey="Manta B" first="Bruno" last="Manta">Bruno Manta</name><affiliation wicri:level="1"><nlm:affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation><affiliation><nlm:affiliation>the Laboratorio de Fisicoquímica Biológica and.</nlm:affiliation><wicri:noCountry code="no comma">the Laboratorio de Fisicoquímica Biológica and.</wicri:noCountry></affiliation></author><author><name sortKey="Moller, Matias N" sort="Moller, Matias N" uniqKey="Moller M" first="Matías N" last="Möller">Matías N. Möller</name><affiliation><nlm:affiliation>the Laboratorio de Fisicoquímica Biológica and.</nlm:affiliation><wicri:noCountry code="no comma">the Laboratorio de Fisicoquímica Biológica and.</wicri:noCountry></affiliation><affiliation><nlm:affiliation>the Center for Free Radical and Biomedical Research, Universidad de la República, Montevideo, Uruguay, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author><author><name sortKey="Bonilla, Mariana" sort="Bonilla, Mariana" uniqKey="Bonilla M" first="Mariana" last="Bonilla">Mariana Bonilla</name><affiliation wicri:level="1"><nlm:affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation><affiliation><nlm:affiliation>the Laboratorio de Fisicoquímica Biológica and.</nlm:affiliation><wicri:noCountry code="no comma">the Laboratorio de Fisicoquímica Biológica and.</wicri:noCountry></affiliation><affiliation wicri:level="1"><nlm:affiliation>Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation></author><author><name sortKey="Deambrosi, Matias" sort="Deambrosi, Matias" uniqKey="Deambrosi M" first="Matías" last="Deambrosi">Matías Deambrosi</name><affiliation wicri:level="1"><nlm:affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation></author><author><name sortKey="Grunberg, Karin" sort="Grunberg, Karin" uniqKey="Grunberg K" first="Karin" last="Grunberg">Karin Grunberg</name><affiliation wicri:level="1"><nlm:affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation><affiliation><nlm:affiliation>the Laboratorio de Fisicoquímica Biológica and.</nlm:affiliation><wicri:noCountry code="no comma">the Laboratorio de Fisicoquímica Biológica and.</wicri:noCountry></affiliation></author><author><name sortKey="Bellanda, Massimo" sort="Bellanda, Massimo" uniqKey="Bellanda M" first="Massimo" last="Bellanda">Massimo Bellanda</name><affiliation wicri:level="4"><nlm:affiliation>the Dipartimento di Scienze Chimiche, Università degli Studi di Padova, Padova 35131, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>the Dipartimento di Scienze Chimiche, Università degli Studi di Padova, Padova 35131</wicri:regionArea><orgName type="university">Université de Padoue</orgName><placeName><settlement type="city">Padoue</settlement><region type="region" nuts="2">Vénétie</region></placeName></affiliation></author><author><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><affiliation wicri:level="1"><nlm:affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400</wicri:regionArea><wicri:noRegion>Montevideo 11400</wicri:noRegion></affiliation></author><author><name sortKey="Ferrer Sueta, Gerardo" sort="Ferrer Sueta, Gerardo" uniqKey="Ferrer Sueta G" first="Gerardo" last="Ferrer-Sueta">Gerardo Ferrer-Sueta</name><affiliation wicri:level="1"><nlm:affiliation>the Laboratorio de Fisicoquímica Biológica and gferrer@fcien.edu.uy.</nlm:affiliation><country wicri:rule="url">Uruguay</country></affiliation><affiliation><nlm:affiliation>the Center for Free Radical and Biomedical Research, Universidad de la República, Montevideo, Uruguay, and.</nlm:affiliation><wicri:noCountry code="subField">and</wicri:noCountry></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Biological Evolution (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Humans (MeSH)</term><term>Kinetics (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Trypanosoma (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cinétique (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Thiols (métabolisme)</term><term>Trypanosoma (métabolisme)</term><term>Évolution biologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Trypanosoma</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Thiols</term><term>Trypanosoma</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biological Evolution</term><term>Catalytic Domain</term><term>Humans</term><term>Kinetics</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cinétique</term><term>Domaine catalytique</term><term>Humains</term><term>Oxydoréduction</term><term>Évolution biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Trypanosomes are flagellated protozoan parasites (kinetoplastids) that have a unique redox metabolism based on the small dithiol trypanothione (T(SH)<sub>2</sub>). Although GSH may still play a biological role in trypanosomatid parasites beyond being a building block of T(SH)<sub>2</sub>, most of its functions are replaced by T(SH)<sub>2</sub> in these organisms. Consequently, trypanosomes have several enzymes adapted to using T(SH)<sub>2</sub> instead of GSH, including the glutaredoxins (Grxs). However, the mechanistic basis of Grx specificity for T(SH)<sub>2</sub> is unknown. Here, we combined fast-kinetic and biophysical approaches, including NMR, MS, and fluorescent tagging, to study the redox function of Grx1, the only cytosolic redox-active Grx in trypanosomes. We observed that Grx1 reduces GSH-containing disulfides (including oxidized trypanothione) in very fast reactions (<i>k</i> > 5 × 10<sup>5</sup> m<sup>-1</sup> s<sup>-1</sup>). We also noted that disulfides without a GSH are much slower oxidants, suggesting a strongly selective binding of the GSH molecule. Not surprisingly, oxidized Grx1 was also reduced very fast by T(SH)<sub>2</sub> (4.8 × 10<sup>6</sup> m<sup>-1</sup> s<sup>-1</sup>); however, GSH-mediated reduction was extremely slow (39 m<sup>-1</sup> s<sup>-1</sup>). This kinetic selectivity in the reduction step of the catalytic cycle suggests that Grx1 uses preferentially a dithiol mechanism, forming a disulfide on the active site during the oxidative half of the catalytic cycle and then being rapidly reduced by T(SH)<sub>2</sub> in the reductive half. Thus, the reduction of glutathionylated substrates avoids GSSG accumulation in an organism lacking GSH reductase. These findings suggest that Grx1 has played an important adaptive role during the rewiring of the thiol-redox metabolism of kinetoplastids.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30593501</PMID><DateCompleted><Year>2019</Year><Month>05</Month><Day>06</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>294</Volume><Issue>9</Issue><PubDate><Year>2019</Year><Month>03</Month><Day>01</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasites.</ArticleTitle><Pagination><MedlinePgn>3235-3248</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA118.006366</ELocationID><Abstract><AbstractText>Trypanosomes are flagellated protozoan parasites (kinetoplastids) that have a unique redox metabolism based on the small dithiol trypanothione (T(SH)<sub>2</sub>). Although GSH may still play a biological role in trypanosomatid parasites beyond being a building block of T(SH)<sub>2</sub>, most of its functions are replaced by T(SH)<sub>2</sub> in these organisms. Consequently, trypanosomes have several enzymes adapted to using T(SH)<sub>2</sub> instead of GSH, including the glutaredoxins (Grxs). However, the mechanistic basis of Grx specificity for T(SH)<sub>2</sub> is unknown. Here, we combined fast-kinetic and biophysical approaches, including NMR, MS, and fluorescent tagging, to study the redox function of Grx1, the only cytosolic redox-active Grx in trypanosomes. We observed that Grx1 reduces GSH-containing disulfides (including oxidized trypanothione) in very fast reactions (<i>k</i> > 5 × 10<sup>5</sup> m<sup>-1</sup> s<sup>-1</sup>). We also noted that disulfides without a GSH are much slower oxidants, suggesting a strongly selective binding of the GSH molecule. Not surprisingly, oxidized Grx1 was also reduced very fast by T(SH)<sub>2</sub> (4.8 × 10<sup>6</sup> m<sup>-1</sup> s<sup>-1</sup>); however, GSH-mediated reduction was extremely slow (39 m<sup>-1</sup> s<sup>-1</sup>). This kinetic selectivity in the reduction step of the catalytic cycle suggests that Grx1 uses preferentially a dithiol mechanism, forming a disulfide on the active site during the oxidative half of the catalytic cycle and then being rapidly reduced by T(SH)<sub>2</sub> in the reductive half. Thus, the reduction of glutathionylated substrates avoids GSSG accumulation in an organism lacking GSH reductase. These findings suggest that Grx1 has played an important adaptive role during the rewiring of the thiol-redox metabolism of kinetoplastids.</AbstractText><CopyrightInformation>© 2019 Manta et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Manta</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Laboratorio de Fisicoquímica Biológica and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Möller</LastName><ForeName>Matías N</ForeName><Initials>MN</Initials><AffiliationInfo><Affiliation>the Laboratorio de Fisicoquímica Biológica and.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Center for Free Radical and Biomedical Research, Universidad de la República, Montevideo, Uruguay, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bonilla</LastName><ForeName>Mariana</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Laboratorio de Fisicoquímica Biológica and.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Deambrosi</LastName><ForeName>Matías</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Laboratorio de Enzimología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Montevideo 11400, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grunberg</LastName><ForeName>Karin</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Laboratorio de Fisicoquímica Biológica and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bellanda</LastName><ForeName>Massimo</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0002-8187-0264</Identifier><AffiliationInfo><Affiliation>the Dipartimento di Scienze Chimiche, Università degli Studi di Padova, Padova 35131, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</Initials><Identifier Source="ORCID">0000-0001-5000-1333</Identifier><AffiliationInfo><Affiliation>From the Grupo Biología Redox de Tripanosomas, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferrer-Sueta</LastName><ForeName>Gerardo</ForeName><Initials>G</Initials><Identifier Source="ORCID">0000-0002-8663-8480</Identifier><AffiliationInfo><Affiliation>the Laboratorio de Fisicoquímica Biológica and gferrer@fcien.edu.uy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>the Center for Free Radical and Biomedical Research, Universidad de la República, Montevideo, Uruguay, and.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2MYG</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal 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