Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity.
Identifieur interne : 000745 ( Main/Exploration ); précédent : 000744; suivant : 000746Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity.
Auteurs : Bruno Manta [Uruguay] ; Carlo Pavan ; Mattia Sturlese ; Andrea Medeiros ; Martina Crispo ; Carsten Berndt ; R Luise Krauth-Siegel ; Massimo Bellanda ; Marcelo A. CominiSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Coenzymes (composition chimique), Cystéine (composition chimique), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Femelle (MeSH), Ferrosulfoprotéines (composition chimique), Glutarédoxines (composition chimique), Glutathion (composition chimique), Liaison aux protéines (MeSH), Maladie du sommeil (parasitologie), Mitochondries (enzymologie), Modèles moléculaires (MeSH), Parasitémie (parasitologie), Protéines de protozoaire (composition chimique), Résonance magnétique nucléaire biomoléculaire (MeSH), Souris (MeSH), Souris de lignée BALB C (MeSH), Structure secondaire des protéines (MeSH), Séquence consensus (MeSH), Séquence d'acides aminés (MeSH), Trypanosoma brucei brucei (enzymologie), Trypanosoma brucei brucei (pathogénicité).
- MESH :
- composition chimique : Coenzymes, Cystéine, Ferrosulfoprotéines, Glutarédoxines, Glutathion, Protéines de protozoaire.
- enzymologie : Mitochondries, Trypanosoma brucei brucei.
- parasitologie : Maladie du sommeil, Parasitémie.
- pathogénicité : Trypanosoma brucei brucei.
- Animaux, Domaine catalytique, Données de séquences moléculaires, Femelle, Liaison aux protéines, Modèles moléculaires, Résonance magnétique nucléaire biomoléculaire, Souris, Souris de lignée BALB C, Structure secondaire des protéines, Séquence consensus, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Catalytic Domain (MeSH), Coenzymes (chemistry), Consensus Sequence (MeSH), Cysteine (chemistry), Female (MeSH), Glutaredoxins (chemistry), Glutathione (chemistry), Iron-Sulfur Proteins (chemistry), Mice (MeSH), Mice, Inbred BALB C (MeSH), Mitochondria (enzymology), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Parasitemia (parasitology), Protein Binding (MeSH), Protein Structure, Secondary (MeSH), Protozoan Proteins (chemistry), Trypanosoma brucei brucei (enzymology), Trypanosoma brucei brucei (pathogenicity), Trypanosomiasis, African (parasitology).
- MESH :
- chemical , chemistry : Coenzymes, Cysteine, Glutaredoxins, Glutathione, Iron-Sulfur Proteins, Protozoan Proteins.
- enzymology : Mitochondria, Trypanosoma brucei brucei.
- parasitology : Parasitemia, Trypanosomiasis, African.
- pathogenicity : Trypanosoma brucei brucei.
- Amino Acid Sequence, Animals, Catalytic Domain, Consensus Sequence, Female, Mice, Mice, Inbred BALB C, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Structure, Secondary.
Abstract
AIMS
Monothiol glutaredoxins (1-C-Grxs) are small proteins linked to the cellular iron and redox metabolism. Trypanosoma brucei brucei, model organism for human African trypanosomiasis, expresses three 1-C-Grxs. 1-C-Grx1 is a highly abundant mitochondrial protein capable to bind an iron-sulfur cluster (ISC) in vitro using glutathione (GSH) as cofactor. We here report on the functional and structural analysis of 1-C-Grx1 in relation to its ISC-binding properties.
RESULTS
An N-terminal extension unique to 1-C-Grx1 from trypanosomatids affects the oligomeric structure and the ISC-binding capacity of the protein. The active-site Cys104 is essential for ISC binding, and the parasite-specific glutathionylspermidine and trypanothione can replace GSH as the ligands of the ISC. Interestingly, trypanothione forms stable protein-free ISC species that in vitro are incorporated into the dithiol T. brucei 2-C-Grx1, but not 1-C-Grx1. Overexpression of the C104S mutant of 1-C-Grx1 impairs disease progression in a mouse model. The structure of the Grx-domain of 1-C-Grx1 was solved by nuclear magnetic resonance spectroscopy. Despite the fact that several residues--which in other 1-C-Grxs are involved in the noncovalent binding of GSH--are conserved, different physicochemical approaches did not reveal any specific interaction between 1-C-Grx1 and free thiol ligands.
INNOVATION
Parasite Grxs are able to coordinate an ISC formed with trypanothione, suggesting a new mechanism of ISC binding and a novel function for the parasite-specific dithiol. The first 3D structure and in vivo relevance of a 1-C-Grx from a pathogenic protozoan are reported.
CONCLUSION
T. brucei 1-C-Grx1 is indispensable for mammalian parasitism and utilizes a new mechanism for ISC binding.
DOI: 10.1089/ars.2012.4859
PubMed: 23259530
PubMed Central: PMC3739951
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Comini</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>Catalytic Domain (MeSH)</term><term>Coenzymes (chemistry)</term><term>Consensus Sequence (MeSH)</term><term>Cysteine (chemistry)</term><term>Female (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutathione (chemistry)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Mice (MeSH)</term><term>Mice, Inbred BALB C (MeSH)</term><term>Mitochondria (enzymology)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term><term>Parasitemia (parasitology)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Protozoan Proteins (chemistry)</term><term>Trypanosoma brucei brucei (enzymology)</term><term>Trypanosoma brucei brucei (pathogenicity)</term><term>Trypanosomiasis, African (parasitology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Coenzymes (composition chimique)</term><term>Cystéine (composition chimique)</term><term>Domaine catalytique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Femelle (MeSH)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Glutarédoxines (composition chimique)</term><term>Glutathion (composition chimique)</term><term>Liaison aux protéines (MeSH)</term><term>Maladie du sommeil (parasitologie)</term><term>Mitochondries (enzymologie)</term><term>Modèles moléculaires (MeSH)</term><term>Parasitémie (parasitologie)</term><term>Protéines de protozoaire (composition chimique)</term><term>Résonance magnétique nucléaire biomoléculaire (MeSH)</term><term>Souris (MeSH)</term><term>Souris de lignée BALB C (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence consensus (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Trypanosoma brucei brucei (enzymologie)</term><term>Trypanosoma brucei brucei (pathogénicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Coenzymes</term><term>Cysteine</term><term>Glutaredoxins</term><term>Glutathione</term><term>Iron-Sulfur Proteins</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Coenzymes</term><term>Cystéine</term><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines de protozoaire</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Mitochondries</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Mitochondria</term><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Maladie du sommeil</term><term>Parasitémie</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Parasitemia</term><term>Trypanosomiasis, African</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Trypanosoma brucei brucei</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Catalytic Domain</term><term>Consensus Sequence</term><term>Female</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Binding</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Femelle</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Structure secondaire des protéines</term><term>Séquence consensus</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>AIMS</b></p><p>Monothiol glutaredoxins (1-C-Grxs) are small proteins linked to the cellular iron and redox metabolism. Trypanosoma brucei brucei, model organism for human African trypanosomiasis, expresses three 1-C-Grxs. 1-C-Grx1 is a highly abundant mitochondrial protein capable to bind an iron-sulfur cluster (ISC) in vitro using glutathione (GSH) as cofactor. We here report on the functional and structural analysis of 1-C-Grx1 in relation to its ISC-binding properties.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>An N-terminal extension unique to 1-C-Grx1 from trypanosomatids affects the oligomeric structure and the ISC-binding capacity of the protein. The active-site Cys104 is essential for ISC binding, and the parasite-specific glutathionylspermidine and trypanothione can replace GSH as the ligands of the ISC. Interestingly, trypanothione forms stable protein-free ISC species that in vitro are incorporated into the dithiol T. brucei 2-C-Grx1, but not 1-C-Grx1. Overexpression of the C104S mutant of 1-C-Grx1 impairs disease progression in a mouse model. The structure of the Grx-domain of 1-C-Grx1 was solved by nuclear magnetic resonance spectroscopy. Despite the fact that several residues--which in other 1-C-Grxs are involved in the noncovalent binding of GSH--are conserved, different physicochemical approaches did not reveal any specific interaction between 1-C-Grx1 and free thiol ligands.</p></div><div type="abstract" xml:lang="en"><p><b>INNOVATION</b></p><p>Parasite Grxs are able to coordinate an ISC formed with trypanothione, suggesting a new mechanism of ISC binding and a novel function for the parasite-specific dithiol. The first 3D structure and in vivo relevance of a 1-C-Grx from a pathogenic protozoan are reported.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>T. brucei 1-C-Grx1 is indispensable for mammalian parasitism and utilizes a new mechanism for ISC binding.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23259530</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>Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity.</ArticleTitle><Pagination><MedlinePgn>665-82</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2012.4859</ELocationID><Abstract><AbstractText Label="AIMS" NlmCategory="OBJECTIVE">Monothiol glutaredoxins (1-C-Grxs) are small proteins linked to the cellular iron and redox metabolism. Trypanosoma brucei brucei, model organism for human African trypanosomiasis, expresses three 1-C-Grxs. 1-C-Grx1 is a highly abundant mitochondrial protein capable to bind an iron-sulfur cluster (ISC) in vitro using glutathione (GSH) as cofactor. We here report on the functional and structural analysis of 1-C-Grx1 in relation to its ISC-binding properties.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">An N-terminal extension unique to 1-C-Grx1 from trypanosomatids affects the oligomeric structure and the ISC-binding capacity of the protein. The active-site Cys104 is essential for ISC binding, and the parasite-specific glutathionylspermidine and trypanothione can replace GSH as the ligands of the ISC. Interestingly, trypanothione forms stable protein-free ISC species that in vitro are incorporated into the dithiol T. brucei 2-C-Grx1, but not 1-C-Grx1. Overexpression of the C104S mutant of 1-C-Grx1 impairs disease progression in a mouse model. The structure of the Grx-domain of 1-C-Grx1 was solved by nuclear magnetic resonance spectroscopy. Despite the fact that several residues--which in other 1-C-Grxs are involved in the noncovalent binding of GSH--are conserved, different physicochemical approaches did not reveal any specific interaction between 1-C-Grx1 and free thiol ligands.</AbstractText><AbstractText Label="INNOVATION" NlmCategory="METHODS">Parasite Grxs are able to coordinate an ISC formed with trypanothione, suggesting a new mechanism of ISC binding and a novel function for the parasite-specific dithiol. The first 3D structure and in vivo relevance of a 1-C-Grx from a pathogenic protozoan are reported.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">T. brucei 1-C-Grx1 is indispensable for mammalian parasitism and utilizes a new mechanism for ISC binding.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Manta</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Montevideo, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pavan</LastName><ForeName>Carlo</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Sturlese</LastName><ForeName>Mattia</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Medeiros</LastName><ForeName>Andrea</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Crispo</LastName><ForeName>Martina</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></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><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</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>2013</Year><Month>02</Month><Day>26</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="D003067">Coenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015800">Protozoan Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</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="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003067" MajorTopicYN="N">Coenzymes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016384" MajorTopicYN="N">Consensus Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008807" MajorTopicYN="N">Mice, Inbred BALB C</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018512" MajorTopicYN="N">Parasitemia</DescriptorName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015800" MajorTopicYN="N">Protozoan Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014346" MajorTopicYN="N">Trypanosoma brucei brucei</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014353" MajorTopicYN="N">Trypanosomiasis, African</DescriptorName><QualifierName 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