[4Fe-4S] cluster trafficking mediated by Arabidopsis mitochondrial ISCA and NFU proteins.
Identifieur interne : 000002 ( Main/Exploration ); précédent : 000001; suivant : 000003[4Fe-4S] cluster trafficking mediated by Arabidopsis mitochondrial ISCA and NFU proteins.
Auteurs : Tamanna Azam [États-Unis] ; Jonathan Przybyla-Toscano [France] ; Florence Vignols [France] ; Jérémy Couturier [France] ; Nicolas Rouhier [France] ; Michael K. Johnson [États-Unis]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2020.
Abstract
Numerous iron-sulfur (Fe-S) proteins with diverse functions are present in the matrix and respiratory chain complexes of mitochondria. Although [4Fe-4S] clusters are the most common type of Fe-S cluster in mitochondria, the molecular mechanism of [4Fe-4S] cluster assembly and insertion into target proteins by the mitochondrial ISC maturation system is not well understood. Here we report a detailed characterization of two late-acting Fe-S cluster carrier proteins from Arabidopsis thaliana, NFU4 and NFU5. Yeast two-hybrid and bimolecular fluorescence complementation studies demonstrated interaction of both the NFU4 and NFU5 proteins with the ISCA class of Fe-S carrier proteins. Recombinant NFU4 and NFU5 were purified as apo-proteins after expression in Escherichia coliIn vitro Fe-S cluster reconstitution led to the insertion of one [4Fe-4S]2+ cluster per homodimer as determined by UV-visible absorption/CD, resonance Raman and EPR spectroscopy, and analytical studies. Cluster transfer reactions, monitored by UV-visible absorption and CD spectroscopy, showed that the [4Fe-4S]2+ cluster-bound ISCA1a/2 heterodimer is effective in transferring [4Fe-4S]2+ clusters to both NFU4 and NFU5 with negligible back reaction. In addition, [4Fe-4S]2+ cluster-bound ISCA1a/2, NFU4 and NFU5 were all found to be effective [4Fe-4S]2+ cluster donors for maturation of the mitochondrial apo-aconitase 2 as assessed by enzyme activity measurements. The results demonstrate rapid, unidirectional and quantitative [4Fe-4S]2+ cluster transfer from ISCA1a/2 to NFU4 or NFU5 that further delineates their respective positions in the plant ISC machinery and their contributions to the maturation of client [4Fe-4S] cluster-containing proteins.
DOI: 10.1074/jbc.RA120.015726
PubMed: 33122194
Affiliations:
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Johnson</name><affiliation wicri:level="1"><nlm:affiliation>Chemistry, University of Georgia, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Chemistry, University of Georgia</wicri:regionArea><wicri:noRegion>University of Georgia</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Numerous iron-sulfur (Fe-S) proteins with diverse functions are present in the matrix and respiratory chain complexes of mitochondria. Although [4Fe-4S] clusters are the most common type of Fe-S cluster in mitochondria, the molecular mechanism of [4Fe-4S] cluster assembly and insertion into target proteins by the mitochondrial ISC maturation system is not well understood. Here we report a detailed characterization of two late-acting Fe-S cluster carrier proteins from <i>Arabidopsis thaliana</i>, NFU4 and NFU5. Yeast two-hybrid and bimolecular fluorescence complementation studies demonstrated interaction of both the NFU4 and NFU5 proteins with the ISCA class of Fe-S carrier proteins. Recombinant NFU4 and NFU5 were purified as apo-proteins after expression in <i>Escherichia coli</i><i>In vitro</i> Fe-S cluster reconstitution led to the insertion of one [4Fe-4S]<sup>2+</sup> cluster per homodimer as determined by UV-visible absorption/CD, resonance Raman and EPR spectroscopy, and analytical studies. Cluster transfer reactions, monitored by UV-visible absorption and CD spectroscopy, showed that the [4Fe-4S]<sup>2+</sup> cluster-bound ISCA1a/2 heterodimer is effective in transferring [4Fe-4S]<sup>2+</sup> clusters to both NFU4 and NFU5 with negligible back reaction. In addition, [4Fe-4S]<sup>2+</sup> cluster-bound ISCA1a/2, NFU4 and NFU5 were all found to be effective [4Fe-4S]<sup>2+</sup> cluster donors for maturation of the mitochondrial apo-aconitase 2 as assessed by enzyme activity measurements. The results demonstrate rapid, unidirectional and quantitative [4Fe-4S]<sup>2+</sup> cluster transfer from ISCA1a/2 to NFU4 or NFU5 that further delineates their respective positions in the plant ISC machinery and their contributions to the maturation of client [4Fe-4S] cluster-containing proteins.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33122194</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Oct</Month><Day>29</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>[4Fe-4S] cluster trafficking mediated by Arabidopsis mitochondrial ISCA and NFU proteins.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">jbc.RA120.015726</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA120.015726</ELocationID><Abstract><AbstractText>Numerous iron-sulfur (Fe-S) proteins with diverse functions are present in the matrix and respiratory chain complexes of mitochondria. Although [4Fe-4S] clusters are the most common type of Fe-S cluster in mitochondria, the molecular mechanism of [4Fe-4S] cluster assembly and insertion into target proteins by the mitochondrial ISC maturation system is not well understood. Here we report a detailed characterization of two late-acting Fe-S cluster carrier proteins from <i>Arabidopsis thaliana</i>, NFU4 and NFU5. Yeast two-hybrid and bimolecular fluorescence complementation studies demonstrated interaction of both the NFU4 and NFU5 proteins with the ISCA class of Fe-S carrier proteins. Recombinant NFU4 and NFU5 were purified as apo-proteins after expression in <i>Escherichia coli</i><i>In vitro</i> Fe-S cluster reconstitution led to the insertion of one [4Fe-4S]<sup>2+</sup> cluster per homodimer as determined by UV-visible absorption/CD, resonance Raman and EPR spectroscopy, and analytical studies. Cluster transfer reactions, monitored by UV-visible absorption and CD spectroscopy, showed that the [4Fe-4S]<sup>2+</sup> cluster-bound ISCA1a/2 heterodimer is effective in transferring [4Fe-4S]<sup>2+</sup> clusters to both NFU4 and NFU5 with negligible back reaction. In addition, [4Fe-4S]<sup>2+</sup> cluster-bound ISCA1a/2, NFU4 and NFU5 were all found to be effective [4Fe-4S]<sup>2+</sup> cluster donors for maturation of the mitochondrial apo-aconitase 2 as assessed by enzyme activity measurements. The results demonstrate rapid, unidirectional and quantitative [4Fe-4S]<sup>2+</sup> cluster transfer from ISCA1a/2 to NFU4 or NFU5 that further delineates their respective positions in the plant ISC machinery and their contributions to the maturation of client [4Fe-4S] cluster-containing proteins.</AbstractText><CopyrightInformation>Published under license by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Azam</LastName><ForeName>Tamanna</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>University of Georgia, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Przybyla-Toscano</LastName><ForeName>Jonathan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Université de Lorraine, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vignols</LastName><ForeName>Florence</ForeName><Initials>F</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-2031-0407</Identifier><AffiliationInfo><Affiliation>Biochimie et Physiologie Moléculaire des Plantes, CNRS/INRA/Université Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-3127-2669</Identifier><AffiliationInfo><Affiliation>Université de Lorraine, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-2036-7884</Identifier><AffiliationInfo><Affiliation>Interaction Arbres Microorganismes, Université de Lorraine, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Michael K</ForeName><Initials>MK</Initials><AffiliationInfo><Affiliation>Chemistry, University of Georgia, United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>10</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Arabidopsis thaliana</Keyword><Keyword MajorTopicYN="N">ISCA proteins</Keyword><Keyword MajorTopicYN="N">NFU proteins</Keyword><Keyword MajorTopicYN="N">Raman spectroscopy</Keyword><Keyword MajorTopicYN="N">circular dichroism (CD)</Keyword><Keyword MajorTopicYN="N">iron-sulfur cluster trafficking</Keyword><Keyword MajorTopicYN="N">iron-sulfur protein</Keyword><Keyword MajorTopicYN="N">mitochondria</Keyword><Keyword MajorTopicYN="N">protein-protein interaction</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>10</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>08</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>10</Month><Day>30</Day><Hour>5</Hour><Minute>44</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>10</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33122194</ArticleId><ArticleId IdType="pii">RA120.015726</ArticleId><ArticleId IdType="doi">10.1074/jbc.RA120.015726</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li><li>États-Unis</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Metz</li><li>Nancy</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><country name="États-Unis"><noRegion><name sortKey="Azam, Tamanna" sort="Azam, Tamanna" uniqKey="Azam T" first="Tamanna" last="Azam">Tamanna Azam</name></noRegion><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name></country><country name="France"><noRegion><name sortKey="Przybyla Toscano, Jonathan" sort="Przybyla Toscano, Jonathan" uniqKey="Przybyla Toscano J" first="Jonathan" last="Przybyla-Toscano">Jonathan Przybyla-Toscano</name></noRegion><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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