GLRX3 Acts as a [2Fe-2S] Cluster Chaperone in the Cytosolic Iron-Sulfur Assembly Machinery Transferring [2Fe-2S] Clusters to NUBP1.
Identifieur interne : 000119 ( Main/Exploration ); précédent : 000118; suivant : 000120GLRX3 Acts as a [2Fe-2S] Cluster Chaperone in the Cytosolic Iron-Sulfur Assembly Machinery Transferring [2Fe-2S] Clusters to NUBP1.
Auteurs : Francesca Camponeschi [Italie] ; Nihar Ranjan Prusty [Italie] ; Sabine Annemarie Elisabeth Heider [Italie] ; Simone Ciofi-Baffoni [Italie] ; Lucia Banci [Italie]Source :
- Journal of the American Chemical Society [ 1520-5126 ] ; 2020.
Abstract
Human cytosolic monothiol glutaredoxin-3 (GLRX3) is a protein essential for the maturation of cytosolic [4Fe-4S] proteins. We show here that dimeric cluster-bridged GLRX3 transfers its [2Fe-2S]2+ clusters to the human P-loop NTPase NUBP1, an essential early component of the cytosolic iron-sulfur assembly (CIA) machinery. Specifically, we observed that [2Fe-2S]2+ clusters are transferred from GLRX3 to monomeric apo NUBP1 and reductively coupled to form [4Fe-4S]2+ clusters on both N-terminal CX13CX2CX5C and C-terminal CPXC motifs of NUBP1 in the presence of glutathione that acts as a reductant. In this process, cluster binding to the C-terminal motif of NUBP1 promotes protein dimerization, while cluster binding to the N-terminal motif does not affect the quaternary structure of NUBP1. The cluster transfer/assembly process is not complete on both N- and C-terminal motifs and indeed requires a reductant stronger than GSH to increase its efficiency. We also showed that the [4Fe-4S]2+ cluster formed at the N-terminal motif of NUBP1 is tightly bound, while the [4Fe-4S]2+ cluster bound at the C-terminal motif is labile. Our findings provide the first evidence for GLRX3 acting as a [2Fe-2S] cluster chaperone in the early stage of the CIA machinery.
DOI: 10.1021/jacs.0c02266
PubMed: 32429669
Affiliations:
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first="Nihar Ranjan" last="Prusty">Nihar Ranjan Prusty</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019</wicri:regionArea><wicri:noRegion>Florence 50019</wicri:noRegion></affiliation></author><author><name sortKey="Heider, Sabine Annemarie Elisabeth" sort="Heider, Sabine Annemarie Elisabeth" uniqKey="Heider S" first="Sabine Annemarie Elisabeth" last="Heider">Sabine Annemarie Elisabeth Heider</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019</wicri:regionArea><wicri:noRegion>Florence 50019</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019</wicri:regionArea><wicri:noRegion>Florence 50019</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, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019</wicri:regionArea><wicri:noRegion>Florence 50019</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019</wicri:regionArea><wicri:noRegion>Florence 50019</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 Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019</wicri:regionArea><wicri:noRegion>Florence 50019</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019</wicri:regionArea><wicri:noRegion>Florence 50019</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of the American Chemical Society</title><idno type="eISSN">1520-5126</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">Human cytosolic monothiol glutaredoxin-3 (GLRX3) is a protein essential for the maturation of cytosolic [4Fe-4S] proteins. We show here that dimeric cluster-bridged GLRX3 transfers its [2Fe-2S]<sup>2+</sup> clusters to the human P-loop NTPase NUBP1, an essential early component of the cytosolic iron-sulfur assembly (CIA) machinery. Specifically, we observed that [2Fe-2S]<sup>2+</sup> clusters are transferred from GLRX3 to monomeric apo NUBP1 and reductively coupled to form [4Fe-4S]<sup>2+</sup> clusters on both N-terminal CX<sub>13</sub>CX<sub>2</sub>CX<sub>5</sub>C and C-terminal CPXC motifs of NUBP1 in the presence of glutathione that acts as a reductant. In this process, cluster binding to the C-terminal motif of NUBP1 promotes protein dimerization, while cluster binding to the N-terminal motif does not affect the quaternary structure of NUBP1. The cluster transfer/assembly process is not complete on both N- and C-terminal motifs and indeed requires a reductant stronger than GSH to increase its efficiency. We also showed that the [4Fe-4S]<sup>2+</sup> cluster formed at the N-terminal motif of NUBP1 is tightly bound, while the [4Fe-4S]<sup>2+</sup> cluster bound at the C-terminal motif is labile. Our findings provide the first evidence for GLRX3 acting as a [2Fe-2S] cluster chaperone in the early stage of the CIA machinery.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32429669</PMID><DateRevised><Year>2020</Year><Month>06</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5126</ISSN><JournalIssue CitedMedium="Internet"><Volume>142</Volume><Issue>24</Issue><PubDate><Year>2020</Year><Month>Jun</Month><Day>17</Day></PubDate></JournalIssue><Title>Journal of the American Chemical Society</Title><ISOAbbreviation>J Am Chem Soc</ISOAbbreviation></Journal><ArticleTitle>GLRX3 Acts as a [2Fe-2S] Cluster Chaperone in the Cytosolic Iron-Sulfur Assembly Machinery Transferring [2Fe-2S] Clusters to NUBP1.</ArticleTitle><Pagination><MedlinePgn>10794-10805</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jacs.0c02266</ELocationID><Abstract><AbstractText>Human cytosolic monothiol glutaredoxin-3 (GLRX3) is a protein essential for the maturation of cytosolic [4Fe-4S] proteins. We show here that dimeric cluster-bridged GLRX3 transfers its [2Fe-2S]<sup>2+</sup> clusters to the human P-loop NTPase NUBP1, an essential early component of the cytosolic iron-sulfur assembly (CIA) machinery. Specifically, we observed that [2Fe-2S]<sup>2+</sup> clusters are transferred from GLRX3 to monomeric apo NUBP1 and reductively coupled to form [4Fe-4S]<sup>2+</sup> clusters on both N-terminal CX<sub>13</sub>CX<sub>2</sub>CX<sub>5</sub>C and C-terminal CPXC motifs of NUBP1 in the presence of glutathione that acts as a reductant. In this process, cluster binding to the C-terminal motif of NUBP1 promotes protein dimerization, while cluster binding to the N-terminal motif does not affect the quaternary structure of NUBP1. The cluster transfer/assembly process is not complete on both N- and C-terminal motifs and indeed requires a reductant stronger than GSH to increase its efficiency. We also showed that the [4Fe-4S]<sup>2+</sup> cluster formed at the N-terminal motif of NUBP1 is tightly bound, while the [4Fe-4S]<sup>2+</sup> cluster bound at the C-terminal motif is labile. Our findings provide the first evidence for GLRX3 acting as a [2Fe-2S] cluster chaperone in the early stage of the CIA machinery.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Camponeschi</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-4122-4508</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prusty</LastName><ForeName>Nihar Ranjan</ForeName><Initials>NR</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-3322-1566</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Heider</LastName><ForeName>Sabine Annemarie Elisabeth</ForeName><Initials>SAE</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-5114-654X</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ciofi-Baffoni</LastName><ForeName>Simone</ForeName><Initials>S</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-2376-3321</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Banci</LastName><ForeName>Lucia</ForeName><Initials>L</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-0562-5774</Identifier><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence, Via della Lastruccia 3, Sesto Fiorentino, Florence 50019, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>06</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Am Chem Soc</MedlineTA><NlmUniqueID>7503056</NlmUniqueID><ISSNLinking>0002-7863</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>5</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>5</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>5</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32429669</ArticleId><ArticleId IdType="doi">10.1021/jacs.0c02266</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Camponeschi, Francesca" sort="Camponeschi, Francesca" uniqKey="Camponeschi F" first="Francesca" last="Camponeschi">Francesca Camponeschi</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="Heider, Sabine Annemarie Elisabeth" sort="Heider, Sabine Annemarie Elisabeth" uniqKey="Heider S" first="Sabine Annemarie Elisabeth" last="Heider">Sabine Annemarie Elisabeth Heider</name><name sortKey="Heider, Sabine Annemarie Elisabeth" sort="Heider, Sabine Annemarie Elisabeth" uniqKey="Heider S" first="Sabine Annemarie Elisabeth" last="Heider">Sabine Annemarie Elisabeth Heider</name><name sortKey="Prusty, Nihar Ranjan" sort="Prusty, Nihar Ranjan" uniqKey="Prusty N" first="Nihar Ranjan" last="Prusty">Nihar Ranjan Prusty</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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