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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Molecular view of an electron transfer process essential for iron–sulfur protein biogenesis</title><author><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></affiliation></author><author><name sortKey="Bertini, Ivano" sort="Bertini, Ivano" uniqKey="Bertini I" first="Ivano" last="Bertini">Ivano Bertini</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Calderone, Vito" sort="Calderone, Vito" uniqKey="Calderone V" first="Vito" last="Calderone">Vito Calderone</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></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><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></affiliation></author><author><name sortKey="Giachetti, Andrea" sort="Giachetti, Andrea" uniqKey="Giachetti A" first="Andrea" last="Giachetti">Andrea Giachetti</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Jaiswal, Deepa" sort="Jaiswal, Deepa" uniqKey="Jaiswal D" first="Deepa" last="Jaiswal">Deepa Jaiswal</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Mikolajczyk, Maciej" sort="Mikolajczyk, Maciej" uniqKey="Mikolajczyk M" first="Maciej" last="Mikolajczyk">Maciej Mikolajczyk</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Piccioli, Mario" sort="Piccioli, Mario" uniqKey="Piccioli M" first="Mario" last="Piccioli">Mario Piccioli</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></affiliation></author><author><name sortKey="Winkelmann, Julia" sort="Winkelmann, Julia" uniqKey="Winkelmann J" first="Julia" last="Winkelmann">Julia Winkelmann</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">23596212</idno><idno type="pmc">3645582</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3645582</idno><idno type="RBID">PMC:3645582</idno><idno type="doi">10.1073/pnas.1302378110</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000292</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000292</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Molecular view of an electron transfer process essential for iron–sulfur protein biogenesis</title><author><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></affiliation></author><author><name sortKey="Bertini, Ivano" sort="Bertini, Ivano" uniqKey="Bertini I" first="Ivano" last="Bertini">Ivano Bertini</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Calderone, Vito" sort="Calderone, Vito" uniqKey="Calderone V" first="Vito" last="Calderone">Vito Calderone</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></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><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></affiliation></author><author><name sortKey="Giachetti, Andrea" sort="Giachetti, Andrea" uniqKey="Giachetti A" first="Andrea" last="Giachetti">Andrea Giachetti</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Jaiswal, Deepa" sort="Jaiswal, Deepa" uniqKey="Jaiswal D" first="Deepa" last="Jaiswal">Deepa Jaiswal</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Mikolajczyk, Maciej" sort="Mikolajczyk, Maciej" uniqKey="Mikolajczyk M" first="Maciej" last="Mikolajczyk">Maciej Mikolajczyk</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author><author><name sortKey="Piccioli, Mario" sort="Piccioli, Mario" uniqKey="Piccioli M" first="Mario" last="Piccioli">Mario Piccioli</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></nlm:aff></affiliation></author><author><name sortKey="Winkelmann, Julia" sort="Winkelmann, Julia" uniqKey="Winkelmann J" first="Julia" last="Winkelmann">Julia Winkelmann</name><affiliation><nlm:aff wicri:cut=" and" id="aff1">Magnetic Resonance Center</nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Biogenesis of iron–sulfur cluster proteins is a highly regulated process that requires complex protein machineries. In the cytosolic iron–sulfur protein assembly machinery, two human key proteins—NADPH-dependent diflavin oxidoreductase 1 (Ndor1) and anamorsin—form a stable complex in vivo that was proposed to provide electrons for assembling cytosolic iron–sulfur cluster proteins. The Ndor1–anamorsin interaction was also suggested to be implicated in the regulation of cell survival/death mechanisms. In the present work we unravel the molecular basis of recognition between Ndor1 and anamorsin and of the electron transfer process. This is based on the structural characterization of the two partner proteins, the investigation of the electron transfer process, and the identification of those protein regions involved in complex formation and those involved in electron transfer. We found that an unstructured region of anamorsin is essential for the formation of a specific and stable protein complex with Ndor1, whereas the C-terminal region of anamorsin, containing the [2Fe-2S] redox center, transiently interacts through complementary charged residues with the FMN-binding site region of Ndor1 to perform electron transfer. Our results propose a molecular model of the electron transfer process that is crucial for understanding the functional role of this interaction in human cells.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="iso-abbrev">Proc. Natl. Acad. Sci. U.S.A</journal-id><journal-id journal-id-type="hwp">pnas</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title-group><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title></journal-title-group><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">23596212</article-id><article-id pub-id-type="pmc">3645582</article-id><article-id pub-id-type="publisher-id">201302378</article-id><article-id pub-id-type="doi">10.1073/pnas.1302378110</article-id><article-categories><subj-group subj-group-type="heading"><subject>Physical Sciences</subject><subj-group><subject>Chemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>Molecular view of an electron transfer process essential for iron–sulfur protein biogenesis</article-title><alt-title alt-title-type="short">Electron transfer between anamorsin and Ndor1</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Banci</surname><given-names>Lucia</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="corresp" rid="cor1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bertini</surname><given-names>Ivano</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="fn" rid="fn1"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Calderone</surname><given-names>Vito</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ciofi-Baffoni</surname><given-names>Simone</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Giachetti</surname><given-names>Andrea</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Jaiswal</surname><given-names>Deepa</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Mikolajczyk</surname><given-names>Maciej</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Piccioli</surname><given-names>Mario</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Winkelmann</surname><given-names>Julia</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><aff id="aff1"><sup>a</sup>Magnetic Resonance Center and</aff><aff id="aff2"><sup>b</sup>Department of Chemistry,<institution>University of Florence</institution>, 50019 Sesto Fiorentino, Florence,<country>Italy</country></aff></contrib-group><author-notes><corresp id="cor1"><sup>1</sup>To whom correspondence should be addressed. E-mail: <email>banci@cerm.unifi.it</email>.</corresp><fn fn-type="edited-by"><p>Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA, and approved March 22, 2013 (received for review February 5, 2013)</p></fn><fn fn-type="con"><p>Author contributions: L.B., I.B., and S.C.-B. designed research; V.C., S.C.-B., A.G., D.J., M.M., M.P., and J.W. performed research; V.C., S.C.-B., A.G., M.M., M.P., and J.W. analyzed data; and L.B., S.C.-B., M.M., M.P., and J.W. wrote the paper.</p></fn></author-notes><pub-date pub-type="ppub"><day>30</day><month>4</month><year>2013</year></pub-date><pub-date pub-type="epub"><day>17</day><month>4</month><year>2013</year></pub-date><volume>110</volume><issue>18</issue><fpage>7136</fpage><lpage>7141</lpage><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="pnas.201302378.pdf"></self-uri><abstract><p>Biogenesis of iron–sulfur cluster proteins is a highly regulated process that requires complex protein machineries. In the cytosolic iron–sulfur protein assembly machinery, two human key proteins—NADPH-dependent diflavin oxidoreductase 1 (Ndor1) and anamorsin—form a stable complex in vivo that was proposed to provide electrons for assembling cytosolic iron–sulfur cluster proteins. The Ndor1–anamorsin interaction was also suggested to be implicated in the regulation of cell survival/death mechanisms. In the present work we unravel the molecular basis of recognition between Ndor1 and anamorsin and of the electron transfer process. This is based on the structural characterization of the two partner proteins, the investigation of the electron transfer process, and the identification of those protein regions involved in complex formation and those involved in electron transfer. We found that an unstructured region of anamorsin is essential for the formation of a specific and stable protein complex with Ndor1, whereas the C-terminal region of anamorsin, containing the [2Fe-2S] redox center, transiently interacts through complementary charged residues with the FMN-binding site region of Ndor1 to perform electron transfer. Our results propose a molecular model of the electron transfer process that is crucial for understanding the functional role of this interaction in human cells.</p></abstract><kwd-group><kwd>Fe/S protein maturation</kwd><kwd>CIAPIN1 domain</kwd><kwd>diflavin reductase</kwd></kwd-group><counts><page-count count="6"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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