CIAO3 protein forms a stable ternary complex with two key players of the human cytosolic iron-sulfur cluster assembly machinery.
Identifieur interne : 000166 ( Main/Exploration ); précédent : 000165; suivant : 000167CIAO3 protein forms a stable ternary complex with two key players of the human cytosolic iron-sulfur cluster assembly machinery.
Auteurs : Vincenzo Maione [Italie] ; Deborah Grifagni [Italie] ; Francesco Torricella [Italie] ; Francesca Cantini [Italie] ; Lucia Banci [Italie]Source :
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [ 1432-1327 ] ; 2020.
Abstract
The CIAO3 protein operates at a crossroad of the cytosolic iron-sulfur protein assembly (CIA) machinery. Although the functional role of CIAO3 has been recently characterized, a description of its interaction network is still not complete. Literature data suggested that CIAO3 interacts individually with CIA2A and CIAO1 protein, with the latter two interacting each other. However, no experimental data are available yet showing the formation of a possible ternary complex composed by CIAO3, CIAO1, and CIA2A. This work shows, for the first time, via size exclusion chromatography coupled with multiangle light scattering, UV-vis absorption and electron paramagnetic resonance (EPR) spectroscopies, the formation of a stable, [4Fe-4S]-bound, complex, composed by CIAO3 and the hetero-CIA2A-CIAO1 complex. Moreover, site-directed mutagenesis data suggested a structural role for the C-terminal [4Fe-4S] cluster of the CIAO3 protein. These findings can provide solid bases for further investigation of the molecular mechanisms involving these CIA machinery proteins.
DOI: 10.1007/s00775-020-01778-z
PubMed: 32222833
Affiliations:
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Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author><author><name sortKey="Grifagni, Deborah" sort="Grifagni, Deborah" uniqKey="Grifagni D" first="Deborah" last="Grifagni">Deborah Grifagni</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author><author><name sortKey="Torricella, Francesco" sort="Torricella, Francesco" uniqKey="Torricella F" first="Francesco" last="Torricella">Francesco Torricella</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author><author><name sortKey="Cantini, Francesca" sort="Cantini, Francesca" uniqKey="Cantini F" first="Francesca" last="Cantini">Francesca Cantini</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. cantini@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy. cantini@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author><author><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. banci@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy. banci@cerm.unifi.it.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino</wicri:regionArea><wicri:noRegion>Sesto Fiorentino</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</title><idno type="eISSN">1432-1327</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">The CIAO3 protein operates at a crossroad of the cytosolic iron-sulfur protein assembly (CIA) machinery. Although the functional role of CIAO3 has been recently characterized, a description of its interaction network is still not complete. Literature data suggested that CIAO3 interacts individually with CIA2A and CIAO1 protein, with the latter two interacting each other. However, no experimental data are available yet showing the formation of a possible ternary complex composed by CIAO3, CIAO1, and CIA2A. This work shows, for the first time, via size exclusion chromatography coupled with multiangle light scattering, UV-vis absorption and electron paramagnetic resonance (EPR) spectroscopies, the formation of a stable, [4Fe-4S]-bound, complex, composed by CIAO3 and the hetero-CIA2A-CIAO1 complex. Moreover, site-directed mutagenesis data suggested a structural role for the C-terminal [4Fe-4S] cluster of the CIAO3 protein. These findings can provide solid bases for further investigation of the molecular mechanisms involving these CIA machinery proteins.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32222833</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-1327</ISSN><JournalIssue CitedMedium="Internet"><Volume>25</Volume><Issue>3</Issue><PubDate><Year>2020</Year><Month>05</Month></PubDate></JournalIssue><Title>Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry</Title><ISOAbbreviation>J Biol Inorg Chem</ISOAbbreviation></Journal><ArticleTitle>CIAO3 protein forms a stable ternary complex with two key players of the human cytosolic iron-sulfur cluster assembly machinery.</ArticleTitle><Pagination><MedlinePgn>501-508</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00775-020-01778-z</ELocationID><Abstract><AbstractText>The CIAO3 protein operates at a crossroad of the cytosolic iron-sulfur protein assembly (CIA) machinery. Although the functional role of CIAO3 has been recently characterized, a description of its interaction network is still not complete. Literature data suggested that CIAO3 interacts individually with CIA2A and CIAO1 protein, with the latter two interacting each other. However, no experimental data are available yet showing the formation of a possible ternary complex composed by CIAO3, CIAO1, and CIA2A. This work shows, for the first time, via size exclusion chromatography coupled with multiangle light scattering, UV-vis absorption and electron paramagnetic resonance (EPR) spectroscopies, the formation of a stable, [4Fe-4S]-bound, complex, composed by CIAO3 and the hetero-CIA2A-CIAO1 complex. Moreover, site-directed mutagenesis data suggested a structural role for the C-terminal [4Fe-4S] cluster of the CIAO3 protein. These findings can provide solid bases for further investigation of the molecular mechanisms involving these CIA machinery proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maione</LastName><ForeName>Vincenzo</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grifagni</LastName><ForeName>Deborah</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Torricella</LastName><ForeName>Francesco</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cantini</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><Identifier Source="ORCID">0000-0003-0526-6732</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. cantini@cerm.unifi.it.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy. cantini@cerm.unifi.it.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Banci</LastName><ForeName>Lucia</ForeName><Initials>L</Initials><Identifier Source="ORCID">0000-0003-0562-5774</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. banci@cerm.unifi.it.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy. banci@cerm.unifi.it.</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>2020</Year><Month>03</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Biol Inorg Chem</MedlineTA><NlmUniqueID>9616326</NlmUniqueID><ISSNLinking>0949-8257</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">CIA machinery</Keyword><Keyword MajorTopicYN="Y">CIA2A</Keyword><Keyword MajorTopicYN="Y">CIAO1</Keyword><Keyword MajorTopicYN="Y">CIAO3</Keyword><Keyword MajorTopicYN="Y">EPR</Keyword><Keyword MajorTopicYN="Y">IOP1</Keyword><Keyword MajorTopicYN="Y">Iron–sulfur protein</Keyword><Keyword MajorTopicYN="Y">NARFL</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>11</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>03</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32222833</ArticleId><ArticleId IdType="doi">10.1007/s00775-020-01778-z</ArticleId><ArticleId IdType="pii">10.1007/s00775-020-01778-z</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Maione, Vincenzo" sort="Maione, Vincenzo" uniqKey="Maione V" first="Vincenzo" last="Maione">Vincenzo Maione</name></noRegion><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><name sortKey="Cantini, Francesca" sort="Cantini, Francesca" uniqKey="Cantini F" first="Francesca" last="Cantini">Francesca Cantini</name><name sortKey="Cantini, Francesca" sort="Cantini, Francesca" uniqKey="Cantini F" first="Francesca" last="Cantini">Francesca Cantini</name><name sortKey="Grifagni, Deborah" sort="Grifagni, Deborah" uniqKey="Grifagni D" first="Deborah" last="Grifagni">Deborah Grifagni</name><name sortKey="Torricella, Francesco" sort="Torricella, Francesco" uniqKey="Torricella F" first="Francesco" last="Torricella">Francesco Torricella</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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