Mitochondrial Arabidopsis thaliana TRXo Isoforms Bind an Iron⁻Sulfur Cluster and Reduce NFU Proteins In Vitro.
Identifieur interne : 000228 ( Main/Exploration ); précédent : 000227; suivant : 000229Mitochondrial Arabidopsis thaliana TRXo Isoforms Bind an Iron⁻Sulfur Cluster and Reduce NFU Proteins In Vitro.
Auteurs : Flavien Zannini [France] ; Thomas Roret [France] ; Jonathan Przybyla-Toscano [France, Suède] ; Tiphaine Dhalleine [France] ; Nicolas Rouhier [France] ; Jérémy Couturier [France]Source :
- Antioxidants (Basel, Switzerland) [ 2076-3921 ] ; 2018.
Abstract
In plants, the mitochondrial thioredoxin (TRX) system generally comprises only one or two isoforms belonging to the TRX h or o classes, being less well developed compared to the numerous isoforms found in chloroplasts. Unlike most other plant species, Arabidopsis thaliana possesses two TRXo isoforms whose physiological functions remain unclear. Here, we performed a structure⁻function analysis to unravel the respective properties of the duplicated TRXo1 and TRXo2 isoforms. Surprisingly, when expressed in Escherichia coli, both recombinant proteins existed in an apo-monomeric form and in a homodimeric iron⁻sulfur (Fe-S) cluster-bridged form. In TRXo2, the [4Fe-4S] cluster is likely ligated in by the usual catalytic cysteines present in the conserved Trp-Cys-Gly-Pro-Cys signature. Solving the three-dimensional structure of both TRXo apo-forms pointed to marked differences in the surface charge distribution, notably in some area usually participating to protein⁻protein interactions with partners. However, we could not detect a difference in their capacity to reduce nitrogen-fixation-subunit-U (NFU)-like proteins, NFU4 or NFU5, two proteins participating in the maturation of certain mitochondrial Fe-S proteins and previously isolated as putative TRXo1 partners. Altogether, these results suggest that a novel regulation mechanism may prevail for mitochondrial TRXs o, possibly existing as a redox-inactive Fe-S cluster-bound form that could be rapidly converted in a redox-active form upon cluster degradation in specific physiological conditions.
DOI: 10.3390/antiox7100142
PubMed: 30322144
PubMed Central: PMC6210436
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Mitochondrial <i>Arabidopsis thaliana</i> TRXo Isoforms Bind an Iron⁻Sulfur Cluster and Reduce NFU Proteins In Vitro.</title><author><name sortKey="Zannini, Flavien" sort="Zannini, Flavien" uniqKey="Zannini F" first="Flavien" last="Zannini">Flavien Zannini</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. flavien.zannini@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. thomas.roret@sb-roscoff.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation><affiliation wicri:level="3"><nlm:affiliation>CNRS, LBI2M, Sorbonne Universités, F-29680 Roscoff, France. thomas.roret@sb-roscoff.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CNRS, LBI2M, Sorbonne Universités, F-29680 Roscoff</wicri:regionArea><placeName><region type="region" nuts="2">Région Bretagne</region><settlement type="city">Roscoff</settlement></placeName></affiliation></author><author><name sortKey="Przybyla Toscano, Jonathan" sort="Przybyla Toscano, Jonathan" uniqKey="Przybyla Toscano J" first="Jonathan" last="Przybyla-Toscano">Jonathan Przybyla-Toscano</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. przybylajonathan@orange.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Plant Physiology, Umeå Plant Science Centre, Umeå University, S-90187 Umea, Sweden. przybylajonathan@orange.fr.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Plant Physiology, Umeå Plant Science Centre, Umeå University, S-90187 Umea</wicri:regionArea><wicri:noRegion>S-90187 Umea</wicri:noRegion></affiliation></author><author><name sortKey="Dhalleine, Tiphaine" sort="Dhalleine, Tiphaine" uniqKey="Dhalleine T" first="Tiphaine" last="Dhalleine">Tiphaine Dhalleine</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. tiphaine.dhalleine@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. nicolas.rouhier@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. jeremy.couturier@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:30322144</idno><idno type="pmid">30322144</idno><idno type="doi">10.3390/antiox7100142</idno><idno type="pmc">PMC6210436</idno><idno type="wicri:Area/Main/Corpus">000204</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000204</idno><idno type="wicri:Area/Main/Curation">000204</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000204</idno><idno type="wicri:Area/Main/Exploration">000204</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Mitochondrial <i>Arabidopsis thaliana</i> TRXo Isoforms Bind an Iron⁻Sulfur Cluster and Reduce NFU Proteins In Vitro.</title><author><name sortKey="Zannini, Flavien" sort="Zannini, Flavien" uniqKey="Zannini F" first="Flavien" last="Zannini">Flavien Zannini</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. flavien.zannini@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. thomas.roret@sb-roscoff.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation><affiliation wicri:level="3"><nlm:affiliation>CNRS, LBI2M, Sorbonne Universités, F-29680 Roscoff, France. thomas.roret@sb-roscoff.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CNRS, LBI2M, Sorbonne Universités, F-29680 Roscoff</wicri:regionArea><placeName><region type="region" nuts="2">Région Bretagne</region><settlement type="city">Roscoff</settlement></placeName></affiliation></author><author><name sortKey="Przybyla Toscano, Jonathan" sort="Przybyla Toscano, Jonathan" uniqKey="Przybyla Toscano J" first="Jonathan" last="Przybyla-Toscano">Jonathan Przybyla-Toscano</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. przybylajonathan@orange.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Plant Physiology, Umeå Plant Science Centre, Umeå University, S-90187 Umea, Sweden. przybylajonathan@orange.fr.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Plant Physiology, Umeå Plant Science Centre, Umeå University, S-90187 Umea</wicri:regionArea><wicri:noRegion>S-90187 Umea</wicri:noRegion></affiliation></author><author><name sortKey="Dhalleine, Tiphaine" sort="Dhalleine, Tiphaine" uniqKey="Dhalleine T" first="Tiphaine" last="Dhalleine">Tiphaine Dhalleine</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. tiphaine.dhalleine@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. nicolas.rouhier@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. jeremy.couturier@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author></analytic><series><title level="j">Antioxidants (Basel, Switzerland)</title><idno type="ISSN">2076-3921</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In plants, the mitochondrial thioredoxin (TRX) system generally comprises only one or two isoforms belonging to the TRX h or o classes, being less well developed compared to the numerous isoforms found in chloroplasts. Unlike most other plant species, <i>Arabidopsis thaliana</i> possesses two TRXo isoforms whose physiological functions remain unclear. Here, we performed a structure⁻function analysis to unravel the respective properties of the duplicated TRXo1 and TRXo2 isoforms. Surprisingly, when expressed in <i>Escherichia coli</i>, both recombinant proteins existed in an apo-monomeric form and in a homodimeric iron⁻sulfur (Fe-S) cluster-bridged form. In TRXo2, the [4Fe-4S] cluster is likely ligated in by the usual catalytic cysteines present in the conserved Trp-Cys-Gly-Pro-Cys signature. Solving the three-dimensional structure of both TRXo apo-forms pointed to marked differences in the surface charge distribution, notably in some area usually participating to protein⁻protein interactions with partners. However, we could not detect a difference in their capacity to reduce nitrogen-fixation-subunit-U (NFU)-like proteins, NFU4 or NFU5, two proteins participating in the maturation of certain mitochondrial Fe-S proteins and previously isolated as putative TRXo1 partners. Altogether, these results suggest that a novel regulation mechanism may prevail for mitochondrial TRXs o, possibly existing as a redox-inactive Fe-S cluster-bound form that could be rapidly converted in a redox-active form upon cluster degradation in specific physiological conditions.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">30322144</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2076-3921</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>10</Issue><PubDate><Year>2018</Year><Month>Oct</Month><Day>13</Day></PubDate></JournalIssue><Title>Antioxidants (Basel, Switzerland)</Title><ISOAbbreviation>Antioxidants (Basel)</ISOAbbreviation></Journal><ArticleTitle>Mitochondrial <i>Arabidopsis thaliana</i> TRXo Isoforms Bind an Iron⁻Sulfur Cluster and Reduce NFU Proteins In Vitro.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E142</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/antiox7100142</ELocationID><Abstract><AbstractText>In plants, the mitochondrial thioredoxin (TRX) system generally comprises only one or two isoforms belonging to the TRX h or o classes, being less well developed compared to the numerous isoforms found in chloroplasts. Unlike most other plant species, <i>Arabidopsis thaliana</i> possesses two TRXo isoforms whose physiological functions remain unclear. Here, we performed a structure⁻function analysis to unravel the respective properties of the duplicated TRXo1 and TRXo2 isoforms. Surprisingly, when expressed in <i>Escherichia coli</i>, both recombinant proteins existed in an apo-monomeric form and in a homodimeric iron⁻sulfur (Fe-S) cluster-bridged form. In TRXo2, the [4Fe-4S] cluster is likely ligated in by the usual catalytic cysteines present in the conserved Trp-Cys-Gly-Pro-Cys signature. Solving the three-dimensional structure of both TRXo apo-forms pointed to marked differences in the surface charge distribution, notably in some area usually participating to protein⁻protein interactions with partners. However, we could not detect a difference in their capacity to reduce nitrogen-fixation-subunit-U (NFU)-like proteins, NFU4 or NFU5, two proteins participating in the maturation of certain mitochondrial Fe-S proteins and previously isolated as putative TRXo1 partners. Altogether, these results suggest that a novel regulation mechanism may prevail for mitochondrial TRXs o, possibly existing as a redox-inactive Fe-S cluster-bound form that could be rapidly converted in a redox-active form upon cluster degradation in specific physiological conditions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zannini</LastName><ForeName>Flavien</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. flavien.zannini@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roret</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. thomas.roret@sb-roscoff.fr.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, LBI2M, Sorbonne Universités, F-29680 Roscoff, France. thomas.roret@sb-roscoff.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Przybyla-Toscano</LastName><ForeName>Jonathan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. przybylajonathan@orange.fr.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Plant Physiology, Umeå Plant Science Centre, Umeå University, S-90187 Umea, Sweden. przybylajonathan@orange.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dhalleine</LastName><ForeName>Tiphaine</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. tiphaine.dhalleine@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. nicolas.rouhier@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0003-3127-2669</Identifier><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France. jeremy.couturier@univ-lorraine.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ANR-11-LABX-0002-01, Lab of Excellence ARBRE</GrantID><Agency>Agence Nationale de la Recherche</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>10</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Antioxidants (Basel)</MedlineTA><NlmUniqueID>101668981</NlmUniqueID><ISSNLinking>2076-3921</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">iron–sulfur cluster</Keyword><Keyword MajorTopicYN="N">mitochondria</Keyword><Keyword MajorTopicYN="N">redox regulation</Keyword><Keyword MajorTopicYN="N">thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>08</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>10</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>10</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>10</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>10</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>10</Month><Day>17</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30322144</ArticleId><ArticleId IdType="pii">antiox7100142</ArticleId><ArticleId IdType="doi">10.3390/antiox7100142</ArticleId><ArticleId IdType="pmc">PMC6210436</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Biochem J. 2012 Aug 1;445(3):337-47</Citation><ArticleIdList><ArticleId IdType="pubmed">22607208</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2011 Aug 5;286(31):27515-27</Citation><ArticleIdList><ArticleId IdType="pubmed">21632542</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 2005 Jul 1;33(Web Server issue):W299-302</Citation><ArticleIdList><ArticleId IdType="pubmed">15980475</ArticleId></ArticleIdList></Reference><Reference><Citation>J Am Chem Soc. 2013 Oct 9;135(40):15153-64</Citation><ArticleIdList><ArticleId IdType="pubmed">24032439</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501</Citation><ArticleIdList><ArticleId IdType="pubmed">20383002</ArticleId></ArticleIdList></Reference><Reference><Citation>Chem Sci. 2015 Dec 1;6(12):7049-7058</Citation><ArticleIdList><ArticleId IdType="pubmed">29861944</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6203-8</Citation><ArticleIdList><ArticleId IdType="pubmed">24733926</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1998 May 19;37(20):7070-6</Citation><ArticleIdList><ArticleId IdType="pubmed">9585516</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Mol Biol. 2017;1653:51-64</Citation><ArticleIdList><ArticleId IdType="pubmed">28822125</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21</Citation><ArticleIdList><ArticleId IdType="pubmed">20057044</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2016 Jun;1857(6):810-8</Citation><ArticleIdList><ArticleId IdType="pubmed">26946085</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2017 Mar 31;12(3):e0174753</Citation><ArticleIdList><ArticleId IdType="pubmed">28362814</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteomics. 2007 Nov;7(22):4158-70</Citation><ArticleIdList><ArticleId IdType="pubmed">17994621</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Plant. 2017 Aug 7;10(8):1107-1125</Citation><ArticleIdList><ArticleId IdType="pubmed">28739495</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Jun 7;102(23):8168-73</Citation><ArticleIdList><ArticleId IdType="pubmed">15917333</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2009 Jun;150(2):646-57</Citation><ArticleIdList><ArticleId IdType="pubmed">19363090</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2015 Mar 17;112(11):E1392-400</Citation><ArticleIdList><ArticleId IdType="pubmed">25646482</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2007 Jun 12;46(23):6903-10</Citation><ArticleIdList><ArticleId IdType="pubmed">17503777</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2017 Apr 18;56(15):2116-2125</Citation><ArticleIdList><ArticleId IdType="pubmed">28358192</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2642-7</Citation><ArticleIdList><ArticleId IdType="pubmed">14983062</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>Nucleic Acids Res. 2007 Jul;35(Web Server issue):W522-5</Citation><ArticleIdList><ArticleId IdType="pubmed">17488841</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Plant. 2009 Mar;2(2):308-22</Citation><ArticleIdList><ArticleId IdType="pubmed">19825616</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2013 Sep 24;52(38):6633-45</Citation><ArticleIdList><ArticleId IdType="pubmed">24032747</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42</Citation><ArticleIdList><ArticleId IdType="pubmed">21460441</ArticleId></ArticleIdList></Reference><Reference><Citation>J Exp Bot. 2017 Feb 1;68(5):1025-1038</Citation><ArticleIdList><ArticleId IdType="pubmed">28184497</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Protoc. 2008;3(7):1171-9</Citation><ArticleIdList><ArticleId IdType="pubmed">18600222</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2005 Jan 17;579(2):337-42</Citation><ArticleIdList><ArticleId IdType="pubmed">15642341</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 1995 Oct 15;3(10):1097-108</Citation><ArticleIdList><ArticleId IdType="pubmed">8590004</ArticleId></ArticleIdList></Reference><Reference><Citation>Metallomics. 2018 Jan 24;10(1):49-72</Citation><ArticleIdList><ArticleId IdType="pubmed">29219157</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell. 2014 Oct 2;56(1):153-62</Citation><ArticleIdList><ArticleId IdType="pubmed">25201412</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Plant. 2013 Sep;6(5):1419-37</Citation><ArticleIdList><ArticleId IdType="pubmed">23702593</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1987 Feb 1;252(2):426-39</Citation><ArticleIdList><ArticleId IdType="pubmed">3028266</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2006 Dec;142(4):1364-79</Citation><ArticleIdList><ArticleId IdType="pubmed">17071643</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2016 Mar;170(3):1284-99</Citation><ArticleIdList><ArticleId IdType="pubmed">26672074</ArticleId></ArticleIdList></Reference><Reference><Citation>Biotechniques. 1995 Aug;19(2):196-8, 200</Citation><ArticleIdList><ArticleId IdType="pubmed">8527135</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2004 Feb 20;303(5661):1185-9</Citation><ArticleIdList><ArticleId IdType="pubmed">14976313</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Sci. 2005 Jul;14(7):1863-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15987909</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6635-40</Citation><ArticleIdList><ArticleId IdType="pubmed">9192617</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1989 Nov 1;182(2):319-26</Citation><ArticleIdList><ArticleId IdType="pubmed">2610349</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):14144-9</Citation><ArticleIdList><ArticleId IdType="pubmed">11717467</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21</Citation><ArticleIdList><ArticleId IdType="pubmed">20124702</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol Biochem. 2004 Apr;42(4):265-71</Citation><ArticleIdList><ArticleId IdType="pubmed">15120110</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2017 Aug 4;292(31):12754-12763</Citation><ArticleIdList><ArticleId IdType="pubmed">28615445</ArticleId></ArticleIdList></Reference><Reference><Citation>Front Plant Sci. 2013 Jul 24;4:259</Citation><ArticleIdList><ArticleId IdType="pubmed">23898337</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Commun. 2017 Apr 04;8:14835</Citation><ArticleIdList><ArticleId IdType="pubmed">28374771</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1994 Jan 28;235(4):1357-63</Citation><ArticleIdList><ArticleId IdType="pubmed">8308900</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2007 May 1;104(18):7379-84</Citation><ArticleIdList><ArticleId IdType="pubmed">17460036</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Plant. 2014 Jan;7(1):156-69</Citation><ArticleIdList><ArticleId IdType="pubmed">24198232</ArticleId></ArticleIdList></Reference><Reference><Citation>J Exp Bot. 2008;59(12):3259-69</Citation><ArticleIdList><ArticleId IdType="pubmed">18632730</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell Physiol. 2013 Jun;54(6):875-92</Citation><ArticleIdList><ArticleId IdType="pubmed">23444301</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2006 Jul 4;45(26):7998-8008</Citation><ArticleIdList><ArticleId IdType="pubmed">16800625</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 1988 Aug 11;16(15):7351-67</Citation><ArticleIdList><ArticleId IdType="pubmed">3045756</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Mol Life Sci. 2009 Aug;66(15):2539-57</Citation><ArticleIdList><ArticleId IdType="pubmed">19506802</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>Gene. 1989 Apr 15;77(1):51-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2744487</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Plants. 2018 Jul;4(7):440-452</Citation><ArticleIdList><ArticleId IdType="pubmed">29915331</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2015 Nov 3;112(44):13735-40</Citation><ArticleIdList><ArticleId IdType="pubmed">26483494</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32</Citation><ArticleIdList><ArticleId IdType="pubmed">20124692</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Apr 1;280(13):12168-80</Citation><ArticleIdList><ArticleId IdType="pubmed">15632145</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2010 Feb 23;107(8):3900-5</Citation><ArticleIdList><ArticleId IdType="pubmed">20133584</ArticleId></ArticleIdList></Reference><Reference><Citation>Antioxid Redox Signal. 2015 Oct 27;:null</Citation><ArticleIdList><ArticleId IdType="pubmed">26381228</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):22-5</Citation><ArticleIdList><ArticleId IdType="pubmed">20057045</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell Environ. 2017 Apr;40(4):553-569</Citation><ArticleIdList><ArticleId IdType="pubmed">26791824</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>France</li><li>Suède</li></country><region><li>Grand Est</li><li>Lorraine (région)</li><li>Région Bretagne</li></region><settlement><li>Nancy</li><li>Roscoff</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><country name="France"><region name="Grand Est"><name sortKey="Zannini, Flavien" sort="Zannini, Flavien" uniqKey="Zannini F" first="Flavien" last="Zannini">Flavien Zannini</name></region><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><name sortKey="Dhalleine, Tiphaine" sort="Dhalleine, Tiphaine" uniqKey="Dhalleine T" first="Tiphaine" last="Dhalleine">Tiphaine Dhalleine</name><name sortKey="Przybyla Toscano, Jonathan" sort="Przybyla Toscano, Jonathan" uniqKey="Przybyla Toscano J" first="Jonathan" last="Przybyla-Toscano">Jonathan Przybyla-Toscano</name><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></country><country name="Suède"><noRegion><name sortKey="Przybyla Toscano, Jonathan" sort="Przybyla Toscano, Jonathan" uniqKey="Przybyla Toscano J" first="Jonathan" last="Przybyla-Toscano">Jonathan Przybyla-Toscano</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/ChloroPlantRedoxV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000228 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000228 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= ChloroPlantRedoxV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:30322144
|texte= Mitochondrial Arabidopsis thaliana TRXo Isoforms Bind an Iron⁻Sulfur Cluster and Reduce NFU Proteins In Vitro.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:30322144" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a ChloroPlantRedoxV1
| This area was generated with Dilib version V0.6.38. |  |