Structural insights into Fe-S protein biogenesis by the CIA targeting complex.
Identifieur interne : 000034 ( Main/Exploration ); précédent : 000033; suivant : 000035Structural insights into Fe-S protein biogenesis by the CIA targeting complex.
Auteurs : Susanne A. Kassube [Suisse] ; Nicolas H. Thom [Suisse]Source :
- Nature structural & molecular biology [ 1545-9985 ] ; 2020.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules HEK293 (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Drosophila (MeSH), Facteurs de transcription (composition chimique), Facteurs de transcription (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Humains (MeSH), Liaison aux protéines (MeSH), Lignée cellulaire (MeSH), Modèles moléculaires (MeSH), Métallochaperons (composition chimique), Métallochaperons (métabolisme), Métalloprotéines (composition chimique), Métalloprotéines (métabolisme), Protéines nucléaires (composition chimique), Protéines nucléaires (métabolisme), Souris (MeSH).
- MESH :
- composition chimique : Facteurs de transcription, Ferrosulfoprotéines, Métallochaperons, Métalloprotéines, Protéines nucléaires.
- métabolisme : Facteurs de transcription, Ferrosulfoprotéines, Métallochaperons, Métalloprotéines, Protéines nucléaires.
- Animaux, Cellules HEK293, Conformation des protéines, Cristallographie aux rayons X, Drosophila, Humains, Liaison aux protéines, Lignée cellulaire, Modèles moléculaires, Souris.
English descriptors
- KwdEn :
- Animals (MeSH), Cell Line (MeSH), Crystallography, X-Ray (MeSH), Drosophila (MeSH), HEK293 Cells (MeSH), Humans (MeSH), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Metallochaperones (chemistry), Metallochaperones (metabolism), Metalloproteins (chemistry), Metalloproteins (metabolism), Mice (MeSH), Models, Molecular (MeSH), Nuclear Proteins (chemistry), Nuclear Proteins (metabolism), Protein Binding (MeSH), Protein Conformation (MeSH), Transcription Factors (chemistry), Transcription Factors (metabolism).
- MESH :
- chemical , chemistry : Iron-Sulfur Proteins, Metallochaperones, Metalloproteins, Nuclear Proteins, Transcription Factors.
- chemical , metabolism : Iron-Sulfur Proteins, Metallochaperones, Metalloproteins, Nuclear Proteins, Transcription Factors.
- Animals, Cell Line, Crystallography, X-Ray, Drosophila, HEK293 Cells, Humans, Mice, Models, Molecular, Protein Binding, Protein Conformation.
Abstract
The cytosolic iron-sulfur (Fe-S) assembly (CIA) pathway is required for the insertion of Fe-S clusters into cytosolic and nuclear client proteins, including many DNA replication and repair factors. The molecular mechanisms of client protein recognition and Fe-S cluster transfer remain unknown. Here, we report crystal structures of the CIA targeting complex (CTC), revealing that its CIAO2B subunit is centrally located and bridges CIAO1 and the client adaptor protein MMS19. Cryo-EM reconstructions of human CTC bound either to the DNA replication factor primase or to the DNA helicase DNA2, combined with biochemical, biophysical and yeast complementation assays, reveal an evolutionarily conserved, bipartite client recognition mode facilitated by CIAO1 and the structural flexibility of the MMS19 subunit. Unexpectedly, the primase Fe-S cluster is located ~70 Å away from the CTC reactive cysteine, implicating conformational dynamics of the CTC or additional maturation factors in the mechanism of Fe-S cluster transfer.
DOI: 10.1038/s41594-020-0454-0
PubMed: 32632277
Affiliations:
Links toward previous steps (curation, corpus...)
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Thom</name><affiliation wicri:level="1"><nlm:affiliation>Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland. nicolas.thoma@fmi.ch.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Friedrich Miescher Institute for Biomedical Research, Basel</wicri:regionArea><wicri:noRegion>Basel</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32632277</idno><idno type="pmid">32632277</idno><idno type="doi">10.1038/s41594-020-0454-0</idno><idno type="wicri:Area/Main/Corpus">000070</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000070</idno><idno type="wicri:Area/Main/Curation">000070</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000070</idno><idno type="wicri:Area/Main/Exploration">000070</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structural insights into Fe-S protein biogenesis by the CIA targeting complex.</title><author><name sortKey="Kassube, Susanne A" sort="Kassube, Susanne A" uniqKey="Kassube S" first="Susanne A" last="Kassube">Susanne A. 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Thom</name><affiliation wicri:level="1"><nlm:affiliation>Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland. nicolas.thoma@fmi.ch.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Friedrich Miescher Institute for Biomedical Research, Basel</wicri:regionArea><wicri:noRegion>Basel</wicri:noRegion></affiliation></author></analytic><series><title level="j">Nature structural & molecular biology</title><idno type="eISSN">1545-9985</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cell Line (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Drosophila (MeSH)</term><term>HEK293 Cells (MeSH)</term><term>Humans (MeSH)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Metallochaperones (chemistry)</term><term>Metallochaperones (metabolism)</term><term>Metalloproteins (chemistry)</term><term>Metalloproteins (metabolism)</term><term>Mice (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Nuclear Proteins (chemistry)</term><term>Nuclear Proteins (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Transcription Factors (chemistry)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules HEK293 (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Drosophila (MeSH)</term><term>Facteurs de transcription (composition chimique)</term><term>Facteurs de transcription (métabolisme)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Métallochaperons (composition chimique)</term><term>Métallochaperons (métabolisme)</term><term>Métalloprotéines (composition chimique)</term><term>Métalloprotéines (métabolisme)</term><term>Protéines nucléaires (composition chimique)</term><term>Protéines nucléaires (métabolisme)</term><term>Souris (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Iron-Sulfur Proteins</term><term>Metallochaperones</term><term>Metalloproteins</term><term>Nuclear Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Iron-Sulfur Proteins</term><term>Metallochaperones</term><term>Metalloproteins</term><term>Nuclear Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Facteurs de transcription</term><term>Ferrosulfoprotéines</term><term>Métallochaperons</term><term>Métalloprotéines</term><term>Protéines nucléaires</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de transcription</term><term>Ferrosulfoprotéines</term><term>Métallochaperons</term><term>Métalloprotéines</term><term>Protéines nucléaires</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Crystallography, X-Ray</term><term>Drosophila</term><term>HEK293 Cells</term><term>Humans</term><term>Mice</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HEK293</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Drosophila</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Modèles moléculaires</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The cytosolic iron-sulfur (Fe-S) assembly (CIA) pathway is required for the insertion of Fe-S clusters into cytosolic and nuclear client proteins, including many DNA replication and repair factors. The molecular mechanisms of client protein recognition and Fe-S cluster transfer remain unknown. Here, we report crystal structures of the CIA targeting complex (CTC), revealing that its CIAO2B subunit is centrally located and bridges CIAO1 and the client adaptor protein MMS19. Cryo-EM reconstructions of human CTC bound either to the DNA replication factor primase or to the DNA helicase DNA2, combined with biochemical, biophysical and yeast complementation assays, reveal an evolutionarily conserved, bipartite client recognition mode facilitated by CIAO1 and the structural flexibility of the MMS19 subunit. Unexpectedly, the primase Fe-S cluster is located ~70 Å away from the CTC reactive cysteine, implicating conformational dynamics of the CTC or additional maturation factors in the mechanism of Fe-S cluster transfer.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32632277</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>09</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1545-9985</ISSN><JournalIssue CitedMedium="Internet"><Volume>27</Volume><Issue>8</Issue><PubDate><Year>2020</Year><Month>08</Month></PubDate></JournalIssue><Title>Nature structural & molecular biology</Title><ISOAbbreviation>Nat Struct Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Structural insights into Fe-S protein biogenesis by the CIA targeting complex.</ArticleTitle><Pagination><MedlinePgn>735-742</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41594-020-0454-0</ELocationID><Abstract><AbstractText>The cytosolic iron-sulfur (Fe-S) assembly (CIA) pathway is required for the insertion of Fe-S clusters into cytosolic and nuclear client proteins, including many DNA replication and repair factors. The molecular mechanisms of client protein recognition and Fe-S cluster transfer remain unknown. Here, we report crystal structures of the CIA targeting complex (CTC), revealing that its CIAO2B subunit is centrally located and bridges CIAO1 and the client adaptor protein MMS19. Cryo-EM reconstructions of human CTC bound either to the DNA replication factor primase or to the DNA helicase DNA2, combined with biochemical, biophysical and yeast complementation assays, reveal an evolutionarily conserved, bipartite client recognition mode facilitated by CIAO1 and the structural flexibility of the MMS19 subunit. Unexpectedly, the primase Fe-S cluster is located ~70 Å away from the CTC reactive cysteine, implicating conformational dynamics of the CTC or additional maturation factors in the mechanism of Fe-S cluster transfer.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kassube</LastName><ForeName>Susanne A</ForeName><Initials>SA</Initials><Identifier Source="ORCID">0000-0003-4322-5886</Identifier><AffiliationInfo><Affiliation>Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thomä</LastName><ForeName>Nicolas H</ForeName><Initials>NH</Initials><Identifier Source="ORCID">0000-0003-2685-906X</Identifier><AffiliationInfo><Affiliation>Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland. nicolas.thoma@fmi.ch.</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>07</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Nat Struct Mol Biol</MedlineTA><NlmUniqueID>101186374</NlmUniqueID><ISSNLinking>1545-9985</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C112111">CIAO1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C569498">CIAO2B protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C416322">MMS19 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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PubStatus="accepted"><Year>2020</Year><Month>05</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>7</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>7</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32632277</ArticleId><ArticleId IdType="doi">10.1038/s41594-020-0454-0</ArticleId><ArticleId IdType="pii">10.1038/s41594-020-0454-0</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><country name="Suisse"><noRegion><name sortKey="Kassube, Susanne A" sort="Kassube, Susanne A" uniqKey="Kassube S" first="Susanne A" last="Kassube">Susanne A. 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