Human glutaredoxin 3 can bind and effectively transfer [4Fe-4S] cluster to apo-iron regulatory protein 1.
Identifieur interne : 000543 ( Main/Exploration ); précédent : 000542; suivant : 000544Human glutaredoxin 3 can bind and effectively transfer [4Fe-4S] cluster to apo-iron regulatory protein 1.
Auteurs : Haiyan Xia [République populaire de Chine] ; Binghua Li [République populaire de Chine] ; Zhou Zhang [République populaire de Chine] ; Qi Wang [République populaire de Chine] ; Tong Qiao [République populaire de Chine] ; Kuanyu Li [République populaire de Chine]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Ferrosulfoprotéines, Protéine-1 de régulation du fer, Protéines de transport.
- synthèse chimique : Aconitate hydratase.
- Humains, Liaison aux protéines, Sites de fixation.
English descriptors
- KwdEn :
- MESH :
- chemical , chemical synthesis : Aconitate Hydratase.
- chemical , chemistry : Carrier Proteins, Iron Regulatory Protein 1, Iron-Sulfur Proteins.
- Binding Sites, Humans, Protein Binding.
Abstract
Glutaredoxin 3 (GLRX3) is a member of monothiol glutaredoxins with a CGFS active site that has been demonstrated to function in cellular iron sensing and trafficking via its bound iron-sulfur cluster. Human GLRX3 has been shown to form a dimer that binds two bridging [2Fe-2S] clusters with glutathione (GSH) as a ligand, assembling a compound 2GLRX3-2[2Fe-2S]-4GSH. Each iron of the iron-sulfur clusters is bound to the thiols of the cysteines, one of which is from the active site of GLRX3, the other from the noncovalently bound GSH. Here, we show that the recombinant human GLRX3 isolated anaerobically from Escherichia coli can incorporate [4Fe-4S] cluster in the absence of GSH, revealed by spectral and enzymatic analysis. [4Fe-4S] cluster-containing GLRX3 is competent for converting iron regulatory protein 1 (apo-IRP1) into aconitase within 30 min, via intact iron-sulfur cluster transfer. These in vitro studies suggest that human GLRX3 is important for cytosolic Fe-S protein maturation.
DOI: 10.1016/j.bbrc.2015.08.073
PubMed: 26296460
Affiliations:
Links toward previous steps (curation, corpus...)
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Electronic address: likuanyu@nju.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Jiangsu Key Laboratory for Molecular Medicine, Medical School of Nanjing University, Nanjing</wicri:regionArea><wicri:noRegion>Nanjing</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aconitate Hydratase (chemical synthesis)</term><term>Binding Sites (MeSH)</term><term>Carrier Proteins (chemistry)</term><term>Humans (MeSH)</term><term>Iron Regulatory Protein 1 (chemistry)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Protein Binding (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aconitate hydratase (synthèse chimique)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Protéine-1 de régulation du fer (composition chimique)</term><term>Protéines de transport (composition chimique)</term><term>Sites de fixation (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Aconitate Hydratase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carrier Proteins</term><term>Iron Regulatory Protein 1</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Protéine-1 de régulation du fer</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Aconitate hydratase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Humans</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Liaison aux protéines</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin 3 (GLRX3) is a member of monothiol glutaredoxins with a CGFS active site that has been demonstrated to function in cellular iron sensing and trafficking via its bound iron-sulfur cluster. Human GLRX3 has been shown to form a dimer that binds two bridging [2Fe-2S] clusters with glutathione (GSH) as a ligand, assembling a compound 2GLRX3-2[2Fe-2S]-4GSH. Each iron of the iron-sulfur clusters is bound to the thiols of the cysteines, one of which is from the active site of GLRX3, the other from the noncovalently bound GSH. Here, we show that the recombinant human GLRX3 isolated anaerobically from Escherichia coli can incorporate [4Fe-4S] cluster in the absence of GSH, revealed by spectral and enzymatic analysis. [4Fe-4S] cluster-containing GLRX3 is competent for converting iron regulatory protein 1 (apo-IRP1) into aconitase within 30 min, via intact iron-sulfur cluster transfer. These in vitro studies suggest that human GLRX3 is important for cytosolic Fe-S protein maturation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26296460</PMID><DateCompleted><Year>2015</Year><Month>11</Month><Day>27</Day></DateCompleted><DateRevised><Year>2015</Year><Month>09</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>465</Volume><Issue>3</Issue><PubDate><Year>2015</Year><Month>Sep</Month><Day>25</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Human glutaredoxin 3 can bind and effectively transfer [4Fe-4S] cluster to apo-iron regulatory protein 1.</ArticleTitle><Pagination><MedlinePgn>620-4</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2015.08.073</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(15)30463-0</ELocationID><Abstract><AbstractText>Glutaredoxin 3 (GLRX3) is a member of monothiol glutaredoxins with a CGFS active site that has been demonstrated to function in cellular iron sensing and trafficking via its bound iron-sulfur cluster. Human GLRX3 has been shown to form a dimer that binds two bridging [2Fe-2S] clusters with glutathione (GSH) as a ligand, assembling a compound 2GLRX3-2[2Fe-2S]-4GSH. Each iron of the iron-sulfur clusters is bound to the thiols of the cysteines, one of which is from the active site of GLRX3, the other from the noncovalently bound GSH. Here, we show that the recombinant human GLRX3 isolated anaerobically from Escherichia coli can incorporate [4Fe-4S] cluster in the absence of GSH, revealed by spectral and enzymatic analysis. [4Fe-4S] cluster-containing GLRX3 is competent for converting iron regulatory protein 1 (apo-IRP1) into aconitase within 30 min, via intact iron-sulfur cluster transfer. These in vitro studies suggest that human GLRX3 is important for cytosolic Fe-S protein maturation.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xia</LastName><ForeName>Haiyan</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Jiangsu Key Laboratory for Molecular Medicine, Medical School of Nanjing University, Nanjing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Binghua</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Jiangsu Key Laboratory for Molecular Medicine, Medical School of Nanjing University, Nanjing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Zhou</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Jiangsu Key Laboratory for Molecular Medicine, Medical School of Nanjing University, Nanjing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Qi</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Department of Vascular Surgery, Nanjing Drum Tower Hospital, Medical School of Nanjing University, Nanjing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qiao</LastName><ForeName>Tong</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Vascular Surgery, Nanjing Drum Tower Hospital, Medical School of Nanjing University, Nanjing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Kuanyu</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Jiangsu Key Laboratory for Molecular Medicine, Medical School of Nanjing University, Nanjing, China. Electronic address: likuanyu@nju.edu.cn.</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>2015</Year><Month>08</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C404105">GLRX3 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="C546175">IRP1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D035941">Iron Regulatory Protein 1</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="Y">chemical synthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D035941" MajorTopicYN="N">Iron Regulatory Protein 1</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutaredoxin 3</Keyword><Keyword MajorTopicYN="N">Glutathione</Keyword><Keyword MajorTopicYN="N">Iron regulatory protein 1</Keyword><Keyword MajorTopicYN="N">Iron–sulfur cluster</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>08</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>08</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>8</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>8</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26296460</ArticleId><ArticleId IdType="pii">S0006-291X(15)30463-0</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2015.08.073</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Xia, Haiyan" sort="Xia, Haiyan" uniqKey="Xia H" first="Haiyan" last="Xia">Haiyan Xia</name></noRegion><name sortKey="Li, Binghua" sort="Li, Binghua" uniqKey="Li B" first="Binghua" last="Li">Binghua Li</name><name sortKey="Li, Kuanyu" sort="Li, Kuanyu" uniqKey="Li K" first="Kuanyu" last="Li">Kuanyu Li</name><name sortKey="Qiao, Tong" sort="Qiao, Tong" uniqKey="Qiao T" first="Tong" last="Qiao">Tong Qiao</name><name sortKey="Wang, Qi" sort="Wang, Qi" uniqKey="Wang Q" first="Qi" last="Wang">Qi Wang</name><name sortKey="Zhang, Zhou" sort="Zhang, Zhou" uniqKey="Zhang Z" first="Zhou" last="Zhang">Zhou Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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