A pathway for assembling [4Fe-4S]2+ clusters in mitochondrial iron-sulfur protein biogenesis.
Identifieur interne : 000181 ( Main/Exploration ); précédent : 000180; suivant : 000182A pathway for assembling [4Fe-4S]2+ clusters in mitochondrial iron-sulfur protein biogenesis.
Auteurs : Veronica Nasta [Italie] ; Dafne Suraci [Italie] ; Spyridon Gourdoupis [Italie] ; Simone Ciofi-Baffoni [Italie] ; Lucia Banci [Italie]Source :
- The FEBS journal [ 1742-4658 ] ; 2020.
Abstract
During its late steps, the mitochondrial iron-sulfur cluster (ISC) assembly machinery leads to the formation of [4Fe-4S] clusters. In vivo studies revealed that several proteins are implicated in the biosynthesis and trafficking of [4Fe-4S] clusters in mitochondria. However, they do not provide a clear picture into how these proteins cooperate. Here, we showed that three late-acting components of the mitochondrial ISC assembly machinery (GLRX5, BOLA3, and NFU1) are part of a ISC assembly pathway leading to the synthesis of a [4Fe-4S]2+ cluster on NFU1. We showed that the [2Fe-2S]2+ GLRX5-BOLA3 complex transfers its cluster to monomeric apo NFU1 to form, in the presence of a reductant, a [4Fe-4S]2+ cluster bound to dimeric NFU1. The cluster formation on NFU1 does not occur with [2Fe-2S]2+ GLRX5, and thus, the [4Fe-4S] cluster assembly pathway is activated only in the presence of BOLA3. These results define NFU1 as an 'assembler' of [4Fe-4S] clusters, that is, a protein able of converting two [2Fe-2S]2+ clusters into a [4Fe-4S]2+ cluster. Finally, we found that the [4Fe-4S]2+ cluster bound to NFU1 has a coordination site which is easily accessible to sulfur-containing ligands, as is typically observed in metallochaperones. This finding supports a role for NFU1 in promoting rapid and controlled cluster-exchange reaction.
DOI: 10.1111/febs.15140
PubMed: 31724821
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of Florence</wicri:noRegion></affiliation></author><author><name sortKey="Suraci, Dafne" sort="Suraci, Dafne" uniqKey="Suraci D" first="Dafne" last="Suraci">Dafne Suraci</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence</wicri:regionArea><wicri:noRegion>University of Florence</wicri:noRegion></affiliation></author><author><name sortKey="Gourdoupis, Spyridon" sort="Gourdoupis, Spyridon" uniqKey="Gourdoupis S" first="Spyridon" last="Gourdoupis">Spyridon Gourdoupis</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence</wicri:regionArea><wicri:noRegion>University of Florence</wicri:noRegion></affiliation></author><author><name sortKey="Ciofi Baffoni, Simone" sort="Ciofi Baffoni, Simone" uniqKey="Ciofi Baffoni S" first="Simone" last="Ciofi-Baffoni">Simone Ciofi-Baffoni</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence</wicri:regionArea><wicri:noRegion>University of Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence</wicri:regionArea><wicri:noRegion>University of Florence</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, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence</wicri:regionArea><wicri:noRegion>University of Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence</wicri:regionArea><wicri:noRegion>University of Florence</wicri:noRegion></affiliation></author></analytic><series><title level="j">The FEBS journal</title><idno type="eISSN">1742-4658</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">During its late steps, the mitochondrial iron-sulfur cluster (ISC) assembly machinery leads to the formation of [4Fe-4S] clusters. In vivo studies revealed that several proteins are implicated in the biosynthesis and trafficking of [4Fe-4S] clusters in mitochondria. However, they do not provide a clear picture into how these proteins cooperate. Here, we showed that three late-acting components of the mitochondrial ISC assembly machinery (GLRX5, BOLA3, and NFU1) are part of a ISC assembly pathway leading to the synthesis of a [4Fe-4S]<sup>2+</sup> cluster on NFU1. We showed that the [2Fe-2S]<sup>2+</sup> GLRX5-BOLA3 complex transfers its cluster to monomeric apo NFU1 to form, in the presence of a reductant, a [4Fe-4S]<sup>2+</sup> cluster bound to dimeric NFU1. The cluster formation on NFU1 does not occur with [2Fe-2S]<sup>2+</sup> GLRX5, and thus, the [4Fe-4S] cluster assembly pathway is activated only in the presence of BOLA3. These results define NFU1 as an 'assembler' of [4Fe-4S] clusters, that is, a protein able of converting two [2Fe-2S]<sup>2+</sup> clusters into a [4Fe-4S]<sup>2+</sup> cluster. Finally, we found that the [4Fe-4S]<sup>2+</sup> cluster bound to NFU1 has a coordination site which is easily accessible to sulfur-containing ligands, as is typically observed in metallochaperones. This finding supports a role for NFU1 in promoting rapid and controlled cluster-exchange reaction.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">31724821</PMID><DateRevised><Year>2020</Year><Month>06</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1742-4658</ISSN><JournalIssue CitedMedium="Internet"><Volume>287</Volume><Issue>11</Issue><PubDate><Year>2020</Year><Month>Jun</Month></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>A pathway for assembling [4Fe-4S]<sup>2+</sup> clusters in mitochondrial iron-sulfur protein biogenesis.</ArticleTitle><Pagination><MedlinePgn>2312-2327</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/febs.15140</ELocationID><Abstract><AbstractText>During its late steps, the mitochondrial iron-sulfur cluster (ISC) assembly machinery leads to the formation of [4Fe-4S] clusters. In vivo studies revealed that several proteins are implicated in the biosynthesis and trafficking of [4Fe-4S] clusters in mitochondria. However, they do not provide a clear picture into how these proteins cooperate. Here, we showed that three late-acting components of the mitochondrial ISC assembly machinery (GLRX5, BOLA3, and NFU1) are part of a ISC assembly pathway leading to the synthesis of a [4Fe-4S]<sup>2+</sup> cluster on NFU1. We showed that the [2Fe-2S]<sup>2+</sup> GLRX5-BOLA3 complex transfers its cluster to monomeric apo NFU1 to form, in the presence of a reductant, a [4Fe-4S]<sup>2+</sup> cluster bound to dimeric NFU1. The cluster formation on NFU1 does not occur with [2Fe-2S]<sup>2+</sup> GLRX5, and thus, the [4Fe-4S] cluster assembly pathway is activated only in the presence of BOLA3. These results define NFU1 as an 'assembler' of [4Fe-4S] clusters, that is, a protein able of converting two [2Fe-2S]<sup>2+</sup> clusters into a [4Fe-4S]<sup>2+</sup> cluster. Finally, we found that the [4Fe-4S]<sup>2+</sup> cluster bound to NFU1 has a coordination site which is easily accessible to sulfur-containing ligands, as is typically observed in metallochaperones. This finding supports a role for NFU1 in promoting rapid and controlled cluster-exchange reaction.</AbstractText><CopyrightInformation>© 2019 Federation of European Biochemical Societies.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nasta</LastName><ForeName>Veronica</ForeName><Initials>V</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-6433-1226</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Suraci</LastName><ForeName>Dafne</ForeName><Initials>D</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-4140-5413</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gourdoupis</LastName><ForeName>Spyridon</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ciofi-Baffoni</LastName><ForeName>Simone</ForeName><Initials>S</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-2376-3321</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Banci</LastName><ForeName>Lucia</ForeName><Initials>L</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-0562-5774</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA15133</GrantID><Agency>European Cooperation in Science and Technology</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>12</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">BOLA3</Keyword><Keyword MajorTopicYN="N">GLRX5</Keyword><Keyword MajorTopicYN="N">NFU1</Keyword><Keyword MajorTopicYN="N">iron-sulfur protein</Keyword><Keyword MajorTopicYN="N">mitochondrial iron-sulfur cluster assembly machinery</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>08</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>10</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>11</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>11</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>11</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>11</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31724821</ArticleId><ArticleId IdType="doi">10.1111/febs.15140</ArticleId></ArticleIdList><ReferenceList><Title>References</Title><Reference><Citation>Braymer JJ & Lill R (2017) Iron-sulfur cluster biogenesis and trafficking in mitochondria. 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CANTINA Verlag, Goldau.</Citation></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Nasta, Veronica" sort="Nasta, Veronica" uniqKey="Nasta V" first="Veronica" last="Nasta">Veronica Nasta</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="Ciofi Baffoni, Simone" sort="Ciofi Baffoni, Simone" uniqKey="Ciofi Baffoni S" first="Simone" last="Ciofi-Baffoni">Simone Ciofi-Baffoni</name><name sortKey="Ciofi Baffoni, Simone" sort="Ciofi Baffoni, Simone" uniqKey="Ciofi Baffoni S" first="Simone" last="Ciofi-Baffoni">Simone Ciofi-Baffoni</name><name sortKey="Gourdoupis, Spyridon" sort="Gourdoupis, Spyridon" uniqKey="Gourdoupis S" first="Spyridon" last="Gourdoupis">Spyridon Gourdoupis</name><name sortKey="Nasta, Veronica" sort="Nasta, Veronica" uniqKey="Nasta V" first="Veronica" last="Nasta">Veronica Nasta</name><name sortKey="Suraci, Dafne" sort="Suraci, Dafne" uniqKey="Suraci D" first="Dafne" last="Suraci">Dafne Suraci</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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