IronSulferCluV1, Main, Exploration, bibRecord, 000070

Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.

Identifieur interne : 000070 ( Main/Exploration ); précédent : 000069; suivant : 000071

Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.

Auteurs : Daniel Trnka [Allemagne] ; Anna D. Engelke [Allemagne] ; Manuela Gellert [Allemagne] ; Anna Moseler [Allemagne, France] ; Md Faruq Hossain [Allemagne] ; Tobias T. Lindenberg [Allemagne] ; Luca Pedroletti [Allemagne] ; Benjamin Odermatt [Allemagne] ; João V. De Souza [Royaume-Uni] ; Agnieszka K. Bronowska [Royaume-Uni] ; Tobias P. Dick [Allemagne] ; Uli Mühlenhoff [Allemagne] ; Andreas J. Meyer [Allemagne] ; Carsten Berndt [Allemagne] ; Christopher Horst Lillig [Allemagne]

Source :

Nature communications [ 2041-1723 ] ; 2020.

RBID : pubmed:32651396

Descripteurs français

KwdFr :
- Animaux (MeSH), Domaine catalytique (MeSH), Ferrosulfoprotéines (composition chimique), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Humains (MeSH), Liaison aux protéines (MeSH), Oxydoréduction (MeSH), Spécificité du substrat (MeSH), Structure secondaire des protéines (MeSH), Transduction du signal (physiologie).
MESH :
- composition chimique : Ferrosulfoprotéines, Glutarédoxines.
- métabolisme : Glutarédoxines.
- physiologie : Transduction du signal.
- Animaux, Domaine catalytique, Humains, Liaison aux protéines, Oxydoréduction, Spécificité du substrat, Structure secondaire des protéines.

English descriptors

KwdEn :
- Animals (MeSH), Catalytic Domain (MeSH), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Humans (MeSH), Iron-Sulfur Proteins (chemistry), Oxidation-Reduction (MeSH), Protein Binding (MeSH), Protein Structure, Secondary (MeSH), Signal Transduction (physiology), Substrate Specificity (MeSH).
MESH :
- chemical , chemistry : Glutaredoxins, Iron-Sulfur Proteins.
- chemical , metabolism : Glutaredoxins.
- physiology : Signal Transduction.
- Animals, Catalytic Domain, Humans, Oxidation-Reduction, Protein Binding, Protein Structure, Secondary, Substrate Specificity.

Abstract

Despite their very close structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) act as oxidoreductases, while CGFS-type (class II) Grxs act as FeS cluster transferases. Here we show that the key determinant of Grx function is a distinct loop structure adjacent to the active site. Engineering of a CxxC/S-type Grx with a CGFS-type loop switched its function from oxidoreductase to FeS transferase. Engineering of a CGFS-type Grx with a CxxC/S-type loop abolished FeS transferase activity and activated the oxidative half reaction of the oxidoreductase. The reductive half-reaction, requiring the interaction with a second GSH molecule, was enabled by switching additional residues in the active site. We explain how subtle structural differences, mostly depending on the structure of one particular loop, act in concert to determine Grx function.

DOI: 10.1038/s41467-020-17323-0
PubMed: 32651396
PubMed Central: PMC7351949

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000065
to stream Main, to step Curation: 000065

Le document en format XML

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<author><name sortKey="Pedroletti, Luca" sort="Pedroletti, Luca" uniqKey="Pedroletti L" first="Luca" last="Pedroletti">Luca Pedroletti</name>
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<author><name sortKey="De Souza, Joao V" sort="De Souza, Joao V" uniqKey="De Souza J" first="João V" last="De Souza">João V. De Souza</name>
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<author><name sortKey="Dick, Tobias P" sort="Dick, Tobias P" uniqKey="Dick T" first="Tobias P" last="Dick">Tobias P. Dick</name>
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<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Division of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), Heidelberg</wicri:regionArea>
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<region type="district" nuts="2">District de Karlsruhe</region>
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<author><name sortKey="Muhlenhoff, Uli" sort="Muhlenhoff, Uli" uniqKey="Muhlenhoff U" first="Uli" last="Mühlenhoff">Uli Mühlenhoff</name>
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<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institute for Cytobiology and Cytopathology, Philipps University Marburg, Marburg</wicri:regionArea>
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<region type="district" nuts="2">District de Giessen</region>
<settlement type="city">Marbourg</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Meyer, Andreas J" sort="Meyer, Andreas J" uniqKey="Meyer A" first="Andreas J" last="Meyer">Andreas J. Meyer</name>
<affiliation wicri:level="3"><nlm:affiliation>Institute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
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<placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region>
<region type="district" nuts="2">District de Cologne</region>
<settlement type="city">Bonn</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name>
<affiliation wicri:level="3"><nlm:affiliation>Department of Neurology, Medical Faculty, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Department of Neurology, Medical Faculty, Heinrich-Heine University Düsseldorf, Düsseldorf</wicri:regionArea>
<placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region>
<region type="district" nuts="2">District de Düsseldorf</region>
<settlement type="city">Düsseldorf</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany. horst@lillig.de.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald</wicri:regionArea>
<wicri:noRegion>Greifswald</wicri:noRegion>
<wicri:noRegion>Greifswald</wicri:noRegion>
<wicri:noRegion>Greifswald</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j">Nature communications</title>
<idno type="eISSN">2041-1723</idno>
<imprint><date when="2020" type="published">2020</date>
</imprint>
</series>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Structure, Secondary (MeSH)</term>
<term>Signal Transduction (physiology)</term>
<term>Substrate Specificity (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Transduction du signal (physiologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Catalytic Domain</term>
<term>Humans</term>
<term>Oxidation-Reduction</term>
<term>Protein Binding</term>
<term>Protein Structure, Secondary</term>
<term>Substrate Specificity</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Domaine catalytique</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Oxydoréduction</term>
<term>Spécificité du substrat</term>
<term>Structure secondaire des protéines</term>
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<front><div type="abstract" xml:lang="en">Despite their very close structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) act as oxidoreductases, while CGFS-type (class II) Grxs act as FeS cluster transferases. Here we show that the key determinant of Grx function is a distinct loop structure adjacent to the active site. Engineering of a CxxC/S-type Grx with a CGFS-type loop switched its function from oxidoreductase to FeS transferase. Engineering of a CGFS-type Grx with a CxxC/S-type loop abolished FeS transferase activity and activated the oxidative half reaction of the oxidoreductase. The reductive half-reaction, requiring the interaction with a second GSH molecule, was enabled by switching additional residues in the active site. We explain how subtle structural differences, mostly depending on the structure of one particular loop, act in concert to determine Grx function.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32651396</PMID>
<DateCompleted><Year>2020</Year>
<Month>08</Month>
<Day>31</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>08</Month>
<Day>31</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>11</Volume>
<Issue>1</Issue>
<PubDate><Year>2020</Year>
<Month>07</Month>
<Day>10</Day>
</PubDate>
</JournalIssue>
<Title>Nature communications</Title>
<ISOAbbreviation>Nat Commun</ISOAbbreviation>
</Journal>
<ArticleTitle>Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.</ArticleTitle>
<Pagination><MedlinePgn>3445</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41467-020-17323-0</ELocationID>
<Abstract><AbstractText>Despite their very close structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) act as oxidoreductases, while CGFS-type (class II) Grxs act as FeS cluster transferases. Here we show that the key determinant of Grx function is a distinct loop structure adjacent to the active site. Engineering of a CxxC/S-type Grx with a CGFS-type loop switched its function from oxidoreductase to FeS transferase. Engineering of a CGFS-type Grx with a CxxC/S-type loop abolished FeS transferase activity and activated the oxidative half reaction of the oxidoreductase. The reductive half-reaction, requiring the interaction with a second GSH molecule, was enabled by switching additional residues in the active site. We explain how subtle structural differences, mostly depending on the structure of one particular loop, act in concert to determine Grx function.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Trnka</LastName>
<ForeName>Daniel</ForeName>
<Initials>D</Initials>
<Identifier Source="ORCID">0000-0002-6609-6880</Identifier>
<AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Engelke</LastName>
<ForeName>Anna D</ForeName>
<Initials>AD</Initials>
<AffiliationInfo><Affiliation>Department of Neurology, Medical Faculty, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gellert</LastName>
<ForeName>Manuela</ForeName>
<Initials>M</Initials>
<Identifier Source="ORCID">0000-0002-2545-7125</Identifier>
<AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Moseler</LastName>
<ForeName>Anna</ForeName>
<Initials>A</Initials>
<Identifier Source="ORCID">0000-0003-4641-8093</Identifier>
<AffiliationInfo><Affiliation>Institute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>UMR 1136 Interactions Arbres/Microorganismes, Université de Lorraine, Vandoeuvre-lès-Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hossain</LastName>
<ForeName>Md Faruq</ForeName>
<Initials>MF</Initials>
<Identifier Source="ORCID">0000-0002-8346-063X</Identifier>
<AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lindenberg</LastName>
<ForeName>Tobias T</ForeName>
<Initials>TT</Initials>
<AffiliationInfo><Affiliation>Institute of Neuroanatomy, University Clinics, University of Bonn, Bonn, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pedroletti</LastName>
<ForeName>Luca</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Institute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Odermatt</LastName>
<ForeName>Benjamin</ForeName>
<Initials>B</Initials>
<Identifier Source="ORCID">0000-0002-9361-2772</Identifier>
<AffiliationInfo><Affiliation>Institute of Neuroanatomy, University Clinics, University of Bonn, Bonn, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>de Souza</LastName>
<ForeName>João V</ForeName>
<Initials>JV</Initials>
<AffiliationInfo><Affiliation>Chemistry, School of Natural and Environmental Sciences, Newcastle University, Newcastle, NE1 7RU, UK.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bronowska</LastName>
<ForeName>Agnieszka K</ForeName>
<Initials>AK</Initials>
<AffiliationInfo><Affiliation>Chemistry, School of Natural and Environmental Sciences, Newcastle University, Newcastle, NE1 7RU, UK.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dick</LastName>
<ForeName>Tobias P</ForeName>
<Initials>TP</Initials>
<Identifier Source="ORCID">0000-0003-1367-973X</Identifier>
<AffiliationInfo><Affiliation>Division of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), Heidelberg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mühlenhoff</LastName>
<ForeName>Uli</ForeName>
<Initials>U</Initials>
<AffiliationInfo><Affiliation>Institute for Cytobiology and Cytopathology, Philipps University Marburg, Marburg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Meyer</LastName>
<ForeName>Andreas J</ForeName>
<Initials>AJ</Initials>
<Identifier Source="ORCID">0000-0001-8144-4364</Identifier>
<AffiliationInfo><Affiliation>Institute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Berndt</LastName>
<ForeName>Carsten</ForeName>
<Initials>C</Initials>
<Identifier Source="ORCID">0000-0001-8583-7966</Identifier>
<AffiliationInfo><Affiliation>Department of Neurology, Medical Faculty, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lillig</LastName>
<ForeName>Christopher Horst</ForeName>
<Initials>CH</Initials>
<Identifier Source="ORCID">0000-0003-2509-5117</Identifier>
<AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany. horst@lillig.de.</Affiliation>
</AffiliationInfo>
</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>2020</Year>
<Month>07</Month>
<Day>10</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Nat Commun</MedlineTA>
<NlmUniqueID>101528555</NlmUniqueID>
<ISSNLinking>2041-1723</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</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="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</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="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName>
</MeshHeading>
</MeshHeadingList>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year>
<Month>10</Month>
<Day>30</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2020</Year>
<Month>06</Month>
<Day>18</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2020</Year>
<Month>7</Month>
<Day>12</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="pubmed"><Year>2020</Year>
<Month>7</Month>
<Day>12</Day>
<Hour>6</Hour>
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<PubMedPubDate PubStatus="medline"><Year>2020</Year>
<Month>9</Month>
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Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.

Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.

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