Monothiol glutaredoxins can bind linear [Fe3S4]+ and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications.
Identifieur interne : 000735 ( Main/Exploration ); précédent : 000734; suivant : 000736Monothiol glutaredoxins can bind linear [Fe3S4]+ and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications.
Auteurs : Bo Zhang [États-Unis] ; Sibali Bandyopadhyay ; Priyanka Shakamuri ; Sunil G. Naik ; Boi Hanh Huynh ; Jérémy Couturier ; Nicolas Rouhier ; Michael K. JohnsonSource :
- Journal of the American Chemical Society [ 1520-5126 ] ; 2013.
Descripteurs français
- KwdFr :
- Aconitate hydratase (métabolisme), Activation enzymatique (MeSH), Analyse spectrale (MeSH), Apoenzymes (métabolisme), Fer (métabolisme), Glutarédoxines (métabolisme), Glutathion (métabolisme), Liaison aux protéines (MeSH), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (enzymologie), Soufre (métabolisme).
- MESH :
- enzymologie : Saccharomyces cerevisiae.
- métabolisme : Aconitate hydratase, Apoenzymes, Fer, Glutarédoxines, Glutathion, Protéines de Saccharomyces cerevisiae, Soufre.
- Activation enzymatique, Analyse spectrale, Liaison aux protéines.
English descriptors
- KwdEn :
- Aconitate Hydratase (metabolism), Apoenzymes (metabolism), Enzyme Activation (MeSH), Glutaredoxins (metabolism), Glutathione (metabolism), Iron (metabolism), Protein Binding (MeSH), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (metabolism), Spectrum Analysis (MeSH), Sulfur (metabolism).
- MESH :
- chemical , metabolism : Aconitate Hydratase, Apoenzymes, Glutaredoxins, Glutathione, Iron, Saccharomyces cerevisiae Proteins, Sulfur.
- enzymology : Saccharomyces cerevisiae.
- Enzyme Activation, Protein Binding, Spectrum Analysis.
Abstract
Saccharomyces cerevisiae mitochondrial glutaredoxin 5 (Grx5) is the archetypical member of a ubiquitous class of monothiol glutaredoxins with a strictly conserved CGFS active-site sequence that has been shown to function in biological [Fe2S2](2+) cluster trafficking. In this work, we show that recombinant S. cerevisiae Grx5 purified aerobically, after prolonged exposure of the cell-free extract to air or after anaerobic reconstitution in the presence of glutathione, predominantly contains a linear [Fe3S4](+) cluster. The excited-state electronic properties and ground-state electronic and vibrational properties of the linear [Fe3S4](+) cluster have been characterized using UV-vis absorption/CD/MCD, EPR, Mössbauer, and resonance Raman spectroscopies. The results reveal a rhombic S = 5/2 linear [Fe3S4](+) cluster with properties similar to those reported for synthetic linear [Fe3S4](+) clusters and the linear [Fe3S4](+) clusters in purple aconitase. Moreover, the results indicate that the Fe-S cluster content previously reported for many monothiol Grxs has been misinterpreted exclusively in terms of [Fe2S2](2+) clusters, rather than linear [Fe3S4](+) clusters or mixtures of linear [Fe3S4](+) and [Fe2S2](2+) clusters. In the absence of GSH, anaerobic reconstitution of Grx5 yields a dimeric form containing one [Fe4S4](2+) cluster that is competent for in vitro activation of apo-aconitase, via intact cluster transfer. The ligation of the linear [Fe3S4](+) and [Fe4S4](2+) clusters in Grx5 has been assessed by spectroscopic, mutational, and analytical studies. Potential roles for monothiol Grx5 in scavenging and recycling linear [Fe3S4](+) clusters released during protein unfolding under oxidative stress conditions and in maturation of [Fe4S4](2+) cluster-containing proteins are discussed in light of these results.
DOI: 10.1021/ja407059n
PubMed: 24032439
PubMed Central: PMC3836218
Affiliations:
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Naik</name></author><author><name sortKey="Huynh, Boi Hanh" sort="Huynh, Boi Hanh" uniqKey="Huynh B" first="Boi Hanh" last="Huynh">Boi Hanh Huynh</name></author><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author><author><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name></author></analytic><series><title level="j">Journal of the American Chemical Society</title><idno type="eISSN">1520-5126</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aconitate Hydratase (metabolism)</term><term>Apoenzymes (metabolism)</term><term>Enzyme Activation (MeSH)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Iron (metabolism)</term><term>Protein Binding (MeSH)</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Spectrum Analysis (MeSH)</term><term>Sulfur (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aconitate hydratase (métabolisme)</term><term>Activation enzymatique (MeSH)</term><term>Analyse spectrale (MeSH)</term><term>Apoenzymes (métabolisme)</term><term>Fer (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Soufre (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aconitate Hydratase</term><term>Apoenzymes</term><term>Glutaredoxins</term><term>Glutathione</term><term>Iron</term><term>Saccharomyces cerevisiae Proteins</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aconitate hydratase</term><term>Apoenzymes</term><term>Fer</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines de Saccharomyces cerevisiae</term><term>Soufre</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme Activation</term><term>Protein Binding</term><term>Spectrum Analysis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Analyse spectrale</term><term>Liaison aux protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Saccharomyces cerevisiae mitochondrial glutaredoxin 5 (Grx5) is the archetypical member of a ubiquitous class of monothiol glutaredoxins with a strictly conserved CGFS active-site sequence that has been shown to function in biological [Fe2S2](2+) cluster trafficking. In this work, we show that recombinant S. cerevisiae Grx5 purified aerobically, after prolonged exposure of the cell-free extract to air or after anaerobic reconstitution in the presence of glutathione, predominantly contains a linear [Fe3S4](+) cluster. The excited-state electronic properties and ground-state electronic and vibrational properties of the linear [Fe3S4](+) cluster have been characterized using UV-vis absorption/CD/MCD, EPR, Mössbauer, and resonance Raman spectroscopies. The results reveal a rhombic S = 5/2 linear [Fe3S4](+) cluster with properties similar to those reported for synthetic linear [Fe3S4](+) clusters and the linear [Fe3S4](+) clusters in purple aconitase. Moreover, the results indicate that the Fe-S cluster content previously reported for many monothiol Grxs has been misinterpreted exclusively in terms of [Fe2S2](2+) clusters, rather than linear [Fe3S4](+) clusters or mixtures of linear [Fe3S4](+) and [Fe2S2](2+) clusters. In the absence of GSH, anaerobic reconstitution of Grx5 yields a dimeric form containing one [Fe4S4](2+) cluster that is competent for in vitro activation of apo-aconitase, via intact cluster transfer. The ligation of the linear [Fe3S4](+) and [Fe4S4](2+) clusters in Grx5 has been assessed by spectroscopic, mutational, and analytical studies. Potential roles for monothiol Grx5 in scavenging and recycling linear [Fe3S4](+) clusters released during protein unfolding under oxidative stress conditions and in maturation of [Fe4S4](2+) cluster-containing proteins are discussed in light of these results. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24032439</PMID><DateCompleted><Year>2014</Year><Month>05</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5126</ISSN><JournalIssue CitedMedium="Internet"><Volume>135</Volume><Issue>40</Issue><PubDate><Year>2013</Year><Month>Oct</Month><Day>09</Day></PubDate></JournalIssue><Title>Journal of the American Chemical Society</Title><ISOAbbreviation>J Am Chem Soc</ISOAbbreviation></Journal><ArticleTitle>Monothiol glutaredoxins can bind linear [Fe3S4]+ and [Fe4S4]2+ clusters in addition to [Fe2S2]2+ clusters: spectroscopic characterization and functional implications.</ArticleTitle><Pagination><MedlinePgn>15153-64</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/ja407059n</ELocationID><Abstract><AbstractText>Saccharomyces cerevisiae mitochondrial glutaredoxin 5 (Grx5) is the archetypical member of a ubiquitous class of monothiol glutaredoxins with a strictly conserved CGFS active-site sequence that has been shown to function in biological [Fe2S2](2+) cluster trafficking. In this work, we show that recombinant S. cerevisiae Grx5 purified aerobically, after prolonged exposure of the cell-free extract to air or after anaerobic reconstitution in the presence of glutathione, predominantly contains a linear [Fe3S4](+) cluster. The excited-state electronic properties and ground-state electronic and vibrational properties of the linear [Fe3S4](+) cluster have been characterized using UV-vis absorption/CD/MCD, EPR, Mössbauer, and resonance Raman spectroscopies. The results reveal a rhombic S = 5/2 linear [Fe3S4](+) cluster with properties similar to those reported for synthetic linear [Fe3S4](+) clusters and the linear [Fe3S4](+) clusters in purple aconitase. Moreover, the results indicate that the Fe-S cluster content previously reported for many monothiol Grxs has been misinterpreted exclusively in terms of [Fe2S2](2+) clusters, rather than linear [Fe3S4](+) clusters or mixtures of linear [Fe3S4](+) and [Fe2S2](2+) clusters. In the absence of GSH, anaerobic reconstitution of Grx5 yields a dimeric form containing one [Fe4S4](2+) cluster that is competent for in vitro activation of apo-aconitase, via intact cluster transfer. The ligation of the linear [Fe3S4](+) and [Fe4S4](2+) clusters in Grx5 has been assessed by spectroscopic, mutational, and analytical studies. Potential roles for monothiol Grx5 in scavenging and recycling linear [Fe3S4](+) clusters released during protein unfolding under oxidative stress conditions and in maturation of [Fe4S4](2+) cluster-containing proteins are discussed in light of these results. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Bo</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia , Athens, Georgia 30602, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bandyopadhyay</LastName><ForeName>Sibali</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Shakamuri</LastName><ForeName>Priyanka</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Naik</LastName><ForeName>Sunil G</ForeName><Initials>SG</Initials></Author><Author ValidYN="Y"><LastName>Huynh</LastName><ForeName>Boi Hanh</ForeName><Initials>BH</Initials></Author><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Michael K</ForeName><Initials>MK</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM047295</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM47295</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM062524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM62524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R37 GM062524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>09</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Am Chem Soc</MedlineTA><NlmUniqueID>7503056</NlmUniqueID><ISSNLinking>0002-7863</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001051">Apoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C528773">Grx5 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001051" MajorTopicYN="N">Apoenzymes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" 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IdType="pubmed">1639790</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Biochem Sci. 2010 Jan;35(1):43-52</Citation><ArticleIdList><ArticleId IdType="pubmed">19811920</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Metab. 2010 Oct 6;12(4):373-85</Citation><ArticleIdList><ArticleId IdType="pubmed">20889129</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Jul 1;280(26):24544-52</Citation><ArticleIdList><ArticleId IdType="pubmed">15833738</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1988;158:357-64</Citation><ArticleIdList><ArticleId IdType="pubmed">3374387</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2012 Jun 5;51(22):4377-89</Citation><ArticleIdList><ArticleId IdType="pubmed">22583368</ArticleId></ArticleIdList></Reference><Reference><Citation>Inorg Chem. 1999 Apr 19;38(8):1847-1865</Citation><ArticleIdList><ArticleId IdType="pubmed">11670957</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 2010 Apr 2;394(2):372-6</Citation><ArticleIdList><ArticleId IdType="pubmed">20226171</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2007 Jun 12;46(23):6804-11</Citation><ArticleIdList><ArticleId IdType="pubmed">17506525</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2009 Oct 13;48(40):9569-81</Citation><ArticleIdList><ArticleId IdType="pubmed">19715344</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2005 Aug 18;436(7053):1035-39</Citation><ArticleIdList><ArticleId IdType="pubmed">16110529</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1997 Aug 1;277(5326):653-9</Citation><ArticleIdList><ArticleId IdType="pubmed">9235882</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2008 Apr 9;27(7):1122-33</Citation><ArticleIdList><ArticleId IdType="pubmed">18354500</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 Jul 11;278(28):25745-51</Citation><ArticleIdList><ArticleId IdType="pubmed">12730244</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1990 May 25;265(15):8533-41</Citation><ArticleIdList><ArticleId IdType="pubmed">2160461</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6087-92</Citation><ArticleIdList><ArticleId IdType="pubmed">9177174</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1984 Dec 10;259(23):14463-71</Citation><ArticleIdList><ArticleId IdType="pubmed">6094558</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1988 Jun 15;263(17):8194-8</Citation><ArticleIdList><ArticleId IdType="pubmed">2836417</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 Oct 4;277(40):37590-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12138088</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2000 Jul 11;39(27):7856-62</Citation><ArticleIdList><ArticleId IdType="pubmed">10891064</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2012 Feb 28;51(8):1687-96</Citation><ArticleIdList><ArticleId IdType="pubmed">22309771</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2011 Oct 18;50(41):8957-69</Citation><ArticleIdList><ArticleId IdType="pubmed">21899261</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Jan 28;275(4):2745-55</Citation><ArticleIdList><ArticleId IdType="pubmed">10644738</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Feb 27;279(9):7785-91</Citation><ArticleIdList><ArticleId IdType="pubmed">14672937</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1999 Aug 10;38(32):10594-605</Citation><ArticleIdList><ArticleId IdType="pubmed">10441157</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2007 Jun 12;46(23):6812-21</Citation><ArticleIdList><ArticleId IdType="pubmed">17506526</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2002 Apr;13(4):1109-21</Citation><ArticleIdList><ArticleId IdType="pubmed">11950925</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2007 Dec 25;46(51):15018-26</Citation><ArticleIdList><ArticleId IdType="pubmed">18044966</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2006 Apr 17;580(9):2273-80</Citation><ArticleIdList><ArticleId IdType="pubmed">16566929</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 2004 Jul 15;427(2):154-63</Citation><ArticleIdList><ArticleId IdType="pubmed">15196989</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2001 Oct 17;123(41):10121-2</Citation><ArticleIdList><ArticleId IdType="pubmed">11592901</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2013 Jun;24(12):1830-41</Citation><ArticleIdList><ArticleId IdType="pubmed">23615440</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2012 Oct 16;51(41):8071-84</Citation><ArticleIdList><ArticleId IdType="pubmed">23003323</ArticleId></ArticleIdList></Reference><Reference><Citation>J Clin Invest. 2010 May;120(5):1749-61</Citation><ArticleIdList><ArticleId IdType="pubmed">20364084</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 2003 Dec;270(23):4736-43</Citation><ArticleIdList><ArticleId IdType="pubmed">14622262</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 May 16;283(20):14092-9</Citation><ArticleIdList><ArticleId IdType="pubmed">18339629</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2012 Sep 19;134(37):15213-6</Citation><ArticleIdList><ArticleId IdType="pubmed">22963613</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 2011 Jan 15;433(2):303-11</Citation><ArticleIdList><ArticleId IdType="pubmed">21029046</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2009 Jul 7;48(26):6041-3</Citation><ArticleIdList><ArticleId IdType="pubmed">19505088</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1999 Dec;19(12):8180-90</Citation><ArticleIdList><ArticleId IdType="pubmed">10567543</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2003 Sep 15;22(18):4815-25</Citation><ArticleIdList><ArticleId IdType="pubmed">12970193</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Cell Biol. 1999 Jul;1(3):130-5</Citation><ArticleIdList><ArticleId IdType="pubmed">10559898</ArticleId></ArticleIdList></Reference><Reference><Citation>Comp Funct Genomics. 2004;5(4):328-41</Citation><ArticleIdList><ArticleId IdType="pubmed">18629168</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 Jul 26;277(30):26944-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12011041</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Apr 4;283(14):8868-76</Citation><ArticleIdList><ArticleId IdType="pubmed">18216016</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Inorg Chem. 2004 Dec;9(8):987-96</Citation><ArticleIdList><ArticleId IdType="pubmed">15578277</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Bandyopadhyay, Sibali" sort="Bandyopadhyay, Sibali" uniqKey="Bandyopadhyay S" first="Sibali" last="Bandyopadhyay">Sibali Bandyopadhyay</name><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><name sortKey="Huynh, Boi Hanh" sort="Huynh, Boi Hanh" uniqKey="Huynh B" first="Boi Hanh" last="Huynh">Boi Hanh Huynh</name><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name><name sortKey="Naik, Sunil G" sort="Naik, Sunil G" uniqKey="Naik S" first="Sunil G" last="Naik">Sunil G. Naik</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Shakamuri, Priyanka" sort="Shakamuri, Priyanka" uniqKey="Shakamuri P" first="Priyanka" last="Shakamuri">Priyanka Shakamuri</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Zhang, Bo" sort="Zhang, Bo" uniqKey="Zhang B" first="Bo" last="Zhang">Bo Zhang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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