GlutaredoxinV1, Main, Exploration, bibRecord, 000588

TtcA a new tRNA-thioltransferase with an Fe-S cluster.

Identifieur interne : 000588 ( Main/Exploration ); précédent : 000587; suivant : 000589

TtcA a new tRNA-thioltransferase with an Fe-S cluster.

Auteurs : Denis Bouvier [France] ; Natty Labessan [France] ; Martin Clémancey [France] ; Jean-Marc Latour [France] ; Jean-Luc Ravanat [France] ; Marc Fontecave [France] ; Mohamed Atta [France]

Source :

Nucleic acids research [ 1362-4962 ] ; 2014.

RBID : pubmed:24914049

Descripteurs français

KwdFr :
- Clonage moléculaire (MeSH), Cystéine (composition chimique), Escherichia coli (enzymologie), Expression des gènes (MeSH), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (isolement et purification), Ferrosulfoprotéines (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (isolement et purification), Glutarédoxines (métabolisme), Protéines Escherichia coli (composition chimique), Protéines Escherichia coli (génétique), Protéines Escherichia coli (isolement et purification), Protéines Escherichia coli (métabolisme), Sulfurtransferases (composition chimique), Sulfurtransferases (génétique), Sulfurtransferases (isolement et purification), Sulfurtransferases (métabolisme).
MESH :
- composition chimique : Cystéine, Ferrosulfoprotéines, Glutarédoxines, Protéines Escherichia coli, Sulfurtransferases.
- enzymologie : Escherichia coli.
- génétique : Ferrosulfoprotéines, Glutarédoxines, Protéines Escherichia coli, Sulfurtransferases.
- isolement et purification : Ferrosulfoprotéines, Glutarédoxines, Protéines Escherichia coli, Sulfurtransferases.
- métabolisme : Ferrosulfoprotéines, Glutarédoxines, Protéines Escherichia coli, Sulfurtransferases.
- Clonage moléculaire, Expression des gènes.

English descriptors

KwdEn :
- Cloning, Molecular (MeSH), Cysteine (chemistry), Escherichia coli (enzymology), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (genetics), Escherichia coli Proteins (isolation & purification), Escherichia coli Proteins (metabolism), Gene Expression (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (isolation & purification), Glutaredoxins (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (isolation & purification), Iron-Sulfur Proteins (metabolism), Sulfurtransferases (chemistry), Sulfurtransferases (genetics), Sulfurtransferases (isolation & purification), Sulfurtransferases (metabolism).
MESH :
- chemical , chemistry : Cysteine, Escherichia coli Proteins, Glutaredoxins, Iron-Sulfur Proteins, Sulfurtransferases.
- enzymology : Escherichia coli.
- chemical , genetics : Escherichia coli Proteins, Glutaredoxins, Iron-Sulfur Proteins, Sulfurtransferases.
- chemical , isolation & purification : Escherichia coli Proteins, Glutaredoxins, Iron-Sulfur Proteins, Sulfurtransferases.
- chemical , metabolism : Escherichia coli Proteins, Glutaredoxins, Iron-Sulfur Proteins, Sulfurtransferases.
- Cloning, Molecular, Gene Expression.

Abstract

TtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Escherichia coli was homologously overexpressed in E. coli. The purified enzyme is a dimer containing an iron-sulfur cluster and displays activity in in vitro assays. The type and properties of the cluster were investigated using a combination of UV-visible absorption, EPR and Mössbauer spectroscopy, as well as by site-directed mutagenesis. These studies demonstrated that the TtcA enzyme contains a redox-active and oxygen-sensitive [4Fe-4S] cluster, chelated by only three cysteine residues and absolutely essential for activity. TtcA is unique tRNA-thiolating enzyme using an iron-sulfur cluster for catalyzing a non-redox reaction.

DOI: 10.1093/nar/gku508
PubMed: 24914049
PubMed Central: PMC4081106

Affiliations:

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

to stream Main, to step Corpus: 000622
to stream Main, to step Curation: 000622

Le document en format XML

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<author><name sortKey="Ravanat, Jean Luc" sort="Ravanat, Jean Luc" uniqKey="Ravanat J" first="Jean-Luc" last="Ravanat">Jean-Luc Ravanat</name>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Fontecave, Marc" sort="Fontecave, Marc" uniqKey="Fontecave M" first="Marc" last="Fontecave">Marc Fontecave</name>
<affiliation wicri:level="3"><nlm:affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France Laboratoire de Chimie des Processus Biologiques, UMR 8229 Collège de France/CNRS/UPMC, 11 place Marcellin-Berthelot, Paris, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France Laboratoire de Chimie des Processus Biologiques, UMR 8229 Collège de France/CNRS/UPMC, 11 place Marcellin-Berthelot, Paris</wicri:regionArea>
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<settlement type="city">Paris</settlement>
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<author><name sortKey="Atta, Mohamed" sort="Atta, Mohamed" uniqKey="Atta M" first="Mohamed" last="Atta">Mohamed Atta</name>
<affiliation wicri:level="3"><nlm:affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France mohamed.atta@cea.fr.</nlm:affiliation>
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<wicri:regionArea>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble</wicri:regionArea>
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<term>Cysteine (chemistry)</term>
<term>Escherichia coli (enzymology)</term>
<term>Escherichia coli Proteins (chemistry)</term>
<term>Escherichia coli Proteins (genetics)</term>
<term>Escherichia coli Proteins (isolation & purification)</term>
<term>Escherichia coli Proteins (metabolism)</term>
<term>Gene Expression (MeSH)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (isolation & purification)</term>
<term>Glutaredoxins (metabolism)</term>
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<term>Iron-Sulfur Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (isolation & purification)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Sulfurtransferases (chemistry)</term>
<term>Sulfurtransferases (genetics)</term>
<term>Sulfurtransferases (isolation & purification)</term>
<term>Sulfurtransferases (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term>
<term>Cystéine (composition chimique)</term>
<term>Escherichia coli (enzymologie)</term>
<term>Expression des gènes (MeSH)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (isolement et purification)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (isolement et purification)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Protéines Escherichia coli (composition chimique)</term>
<term>Protéines Escherichia coli (génétique)</term>
<term>Protéines Escherichia coli (isolement et purification)</term>
<term>Protéines Escherichia coli (métabolisme)</term>
<term>Sulfurtransferases (composition chimique)</term>
<term>Sulfurtransferases (génétique)</term>
<term>Sulfurtransferases (isolement et purification)</term>
<term>Sulfurtransferases (métabolisme)</term>
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<term>Escherichia coli Proteins</term>
<term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
<term>Sulfurtransferases</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Protéines Escherichia coli</term>
<term>Sulfurtransferases</term>
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</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Escherichia coli Proteins</term>
<term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
<term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Protéines Escherichia coli</term>
<term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Escherichia coli Proteins</term>
<term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
<term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Protéines Escherichia coli</term>
<term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Escherichia coli Proteins</term>
<term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
<term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Protéines Escherichia coli</term>
<term>Sulfurtransferases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term>
<term>Gene Expression</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term>
<term>Expression des gènes</term>
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<front><div type="abstract" xml:lang="en">TtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Escherichia coli was homologously overexpressed in E. coli. The purified enzyme is a dimer containing an iron-sulfur cluster and displays activity in in vitro assays. The type and properties of the cluster were investigated using a combination of UV-visible absorption, EPR and Mössbauer spectroscopy, as well as by site-directed mutagenesis. These studies demonstrated that the TtcA enzyme contains a redox-active and oxygen-sensitive [4Fe-4S] cluster, chelated by only three cysteine residues and absolutely essential for activity. TtcA is unique tRNA-thiolating enzyme using an iron-sulfur cluster for catalyzing a non-redox reaction. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24914049</PMID>
<DateCompleted><Year>2014</Year>
<Month>09</Month>
<Day>02</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1362-4962</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>42</Volume>
<Issue>12</Issue>
<PubDate><Year>2014</Year>
<Month>Jul</Month>
</PubDate>
</JournalIssue>
<Title>Nucleic acids research</Title>
<ISOAbbreviation>Nucleic Acids Res</ISOAbbreviation>
</Journal>
<ArticleTitle>TtcA a new tRNA-thioltransferase with an Fe-S cluster.</ArticleTitle>
<Pagination><MedlinePgn>7960-70</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1093/nar/gku508</ELocationID>
<Abstract><AbstractText>TtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Escherichia coli was homologously overexpressed in E. coli. The purified enzyme is a dimer containing an iron-sulfur cluster and displays activity in in vitro assays. The type and properties of the cluster were investigated using a combination of UV-visible absorption, EPR and Mössbauer spectroscopy, as well as by site-directed mutagenesis. These studies demonstrated that the TtcA enzyme contains a redox-active and oxygen-sensitive [4Fe-4S] cluster, chelated by only three cysteine residues and absolutely essential for activity. TtcA is unique tRNA-thiolating enzyme using an iron-sulfur cluster for catalyzing a non-redox reaction. </AbstractText>
<CopyrightInformation>© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bouvier</LastName>
<ForeName>Denis</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Labessan</LastName>
<ForeName>Natty</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Clémancey</LastName>
<ForeName>Martin</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Latour</LastName>
<ForeName>Jean-Marc</ForeName>
<Initials>JM</Initials>
<AffiliationInfo><Affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ravanat</LastName>
<ForeName>Jean-Luc</ForeName>
<Initials>JL</Initials>
<AffiliationInfo><Affiliation>University of Grenoble Alpes, INAC, SCIB, F-38000 Grenoble, France CEA, iNAC, SCIB, F-38054 Grenoble, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fontecave</LastName>
<ForeName>Marc</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France Laboratoire de Chimie des Processus Biologiques, UMR 8229 Collège de France/CNRS/UPMC, 11 place Marcellin-Berthelot, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Atta</LastName>
<ForeName>Mohamed</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>University of Grenoble Alpes, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CNRS, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France CEA, iRTSV-LCBM, UMR5249, F-38000 Grenoble, France mohamed.atta@cea.fr.</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>2014</Year>
<Month>06</Month>
<Day>09</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Nucleic Acids Res</MedlineTA>
<NlmUniqueID>0411011</NlmUniqueID>
<ISSNLinking>0305-1048</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.8.1.-</RegistryNumber>
<NameOfSubstance UI="D013466">Sulfurtransferases</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.8.1.-</RegistryNumber>
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<Chemical><RegistryNumber>K848JZ4886</RegistryNumber>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029968" MajorTopicYN="N">Escherichia coli Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName>
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<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
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TtcA a new tRNA-thioltransferase with an Fe-S cluster.

TtcA a new tRNA-thioltransferase with an Fe-S cluster.

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