Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein.
Identifieur interne : 000A49 ( Main/Exploration ); précédent : 000A48; suivant : 000A50Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein.
Auteurs : Petra Haunhorst [Allemagne] ; Carsten Berndt ; Susanne Eitner ; José R. Godoy ; Christopher Horst LilligSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2010.
Descripteurs français
- KwdFr :
- Cellules Jurkat (MeSH), Conformation des protéines (MeSH), Fer (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Hexacyanoferrates III (métabolisme), Humains (MeSH), Immunoprécipitation (MeSH), Oxydoréduction (MeSH), Protéines de transport (composition chimique), Protéines de transport (métabolisme), Radio-isotopes du fer (métabolisme), S-Nitroso-glutathion (métabolisme), Stabilité protéique (MeSH), Structure tertiaire des protéines (MeSH).
- MESH :
- composition chimique : Ferrosulfoprotéines, Protéines de transport.
- métabolisme : Fer, Ferrosulfoprotéines, Hexacyanoferrates III, Protéines de transport, Radio-isotopes du fer, S-Nitroso-glutathion.
- Cellules Jurkat, Conformation des protéines, Humains, Immunoprécipitation, Oxydoréduction, Stabilité protéique, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Carrier Proteins (chemistry), Carrier Proteins (metabolism), Ferricyanides (metabolism), Humans (MeSH), Immunoprecipitation (MeSH), Iron (metabolism), Iron Radioisotopes (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Jurkat Cells (MeSH), Oxidation-Reduction (MeSH), Protein Conformation (MeSH), Protein Stability (MeSH), Protein Structure, Tertiary (MeSH), S-Nitrosoglutathione (metabolism).
- MESH :
- chemical , chemistry : Carrier Proteins, Iron-Sulfur Proteins.
- chemical , metabolism : Carrier Proteins, Ferricyanides, Iron, Iron Radioisotopes, Iron-Sulfur Proteins, S-Nitrosoglutathione.
- Humans, Immunoprecipitation, Jurkat Cells, Oxidation-Reduction, Protein Conformation, Protein Stability, Protein Structure, Tertiary.
Abstract
Mammalian glutaredoxin 3 (Grx3/PICOT) is an essential protein involved in the regulation of signal transduction, for instance during immune cell activation and development of cardiac hypertrophy, presumably in response to redox signals. This function requires the sensing of such stresses by a hitherto unknown mechanism. Here, we characterized Grx3/PICOT as iron-sulfur protein. The protein binds two bridging [2Fe-2S] clusters in a homodimeric complex with the active site cysteinyl residues of its two monothiol glutaredoxin domains and glutathione bound non-covalently to the Grx domains. Co-immunoprecipitation of 55-iron with Grx3/PICOT from Jurkat cells suggested the presence of these cofactors under physiological conditions. The [2Fe-2S]2+ clusters were not redox active, instead they were lost upon treatment of the holo protein with ferricyanide or S-nitroso glutathione. This redox-induced dissociation of the Grx3/PICOT holo complex may be a mechanism of Grx3/PICOT activation in response to reactive oxygen and nitrogen species.
DOI: 10.1016/j.bbrc.2010.03.016
PubMed: 20226171
Affiliations:
Links toward previous steps (curation, corpus...)
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Godoy</name></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carrier Proteins (chemistry)</term><term>Carrier Proteins (metabolism)</term><term>Ferricyanides (metabolism)</term><term>Humans (MeSH)</term><term>Immunoprecipitation (MeSH)</term><term>Iron (metabolism)</term><term>Iron Radioisotopes (metabolism)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Jurkat Cells (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Stability (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>S-Nitrosoglutathione (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules Jurkat (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Hexacyanoferrates III (métabolisme)</term><term>Humains (MeSH)</term><term>Immunoprécipitation (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de transport (composition chimique)</term><term>Protéines de transport (métabolisme)</term><term>Radio-isotopes du fer (métabolisme)</term><term>S-Nitroso-glutathion (métabolisme)</term><term>Stabilité protéique (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carrier Proteins</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term><term>Ferricyanides</term><term>Iron</term><term>Iron Radioisotopes</term><term>Iron-Sulfur Proteins</term><term>S-Nitrosoglutathione</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fer</term><term>Ferrosulfoprotéines</term><term>Hexacyanoferrates III</term><term>Protéines de transport</term><term>Radio-isotopes du fer</term><term>S-Nitroso-glutathion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Immunoprecipitation</term><term>Jurkat Cells</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Protein Stability</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules Jurkat</term><term>Conformation des protéines</term><term>Humains</term><term>Immunoprécipitation</term><term>Oxydoréduction</term><term>Stabilité protéique</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mammalian glutaredoxin 3 (Grx3/PICOT) is an essential protein involved in the regulation of signal transduction, for instance during immune cell activation and development of cardiac hypertrophy, presumably in response to redox signals. This function requires the sensing of such stresses by a hitherto unknown mechanism. Here, we characterized Grx3/PICOT as iron-sulfur protein. The protein binds two bridging [2Fe-2S] clusters in a homodimeric complex with the active site cysteinyl residues of its two monothiol glutaredoxin domains and glutathione bound non-covalently to the Grx domains. Co-immunoprecipitation of 55-iron with Grx3/PICOT from Jurkat cells suggested the presence of these cofactors under physiological conditions. The [2Fe-2S]2+ clusters were not redox active, instead they were lost upon treatment of the holo protein with ferricyanide or S-nitroso glutathione. This redox-induced dissociation of the Grx3/PICOT holo complex may be a mechanism of Grx3/PICOT activation in response to reactive oxygen and nitrogen species.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20226171</PMID><DateCompleted><Year>2010</Year><Month>04</Month><Day>22</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>394</Volume><Issue>2</Issue><PubDate><Year>2010</Year><Month>Apr</Month><Day>02</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein.</ArticleTitle><Pagination><MedlinePgn>372-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2010.03.016</ELocationID><Abstract><AbstractText>Mammalian glutaredoxin 3 (Grx3/PICOT) is an essential protein involved in the regulation of signal transduction, for instance during immune cell activation and development of cardiac hypertrophy, presumably in response to redox signals. This function requires the sensing of such stresses by a hitherto unknown mechanism. Here, we characterized Grx3/PICOT as iron-sulfur protein. The protein binds two bridging [2Fe-2S] clusters in a homodimeric complex with the active site cysteinyl residues of its two monothiol glutaredoxin domains and glutathione bound non-covalently to the Grx domains. Co-immunoprecipitation of 55-iron with Grx3/PICOT from Jurkat cells suggested the presence of these cofactors under physiological conditions. The [2Fe-2S]2+ clusters were not redox active, instead they were lost upon treatment of the holo protein with ferricyanide or S-nitroso glutathione. This redox-induced dissociation of the Grx3/PICOT holo complex may be a mechanism of Grx3/PICOT activation in response to reactive oxygen and nitrogen species.</AbstractText><CopyrightInformation>2010 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Haunhorst</LastName><ForeName>Petra</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institut für Klinische Zytobiologie und Zytopathologie, Fachbereich Medizin, Philipps Universität Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Eitner</LastName><ForeName>Susanne</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Godoy</LastName><ForeName>José R</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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PubStatus="pubmed"><Year>2010</Year><Month>3</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>4</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20226171</ArticleId><ArticleId IdType="pii">S0006-291X(10)00453-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2010.03.016</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name><name sortKey="Eitner, Susanne" sort="Eitner, Susanne" uniqKey="Eitner S" first="Susanne" last="Eitner">Susanne Eitner</name><name sortKey="Godoy, Jose R" sort="Godoy, Jose R" uniqKey="Godoy J" first="José R" last="Godoy">José R. Godoy</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Haunhorst, Petra" sort="Haunhorst, Petra" uniqKey="Haunhorst P" first="Petra" last="Haunhorst">Petra Haunhorst</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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