Elucidating the Molecular Function of Human BOLA2 in GRX3-Dependent Anamorsin Maturation Pathway.
Identifieur interne : 000563 ( Main/Exploration ); précédent : 000562; suivant : 000564Elucidating the Molecular Function of Human BOLA2 in GRX3-Dependent Anamorsin Maturation Pathway.
Auteurs : Lucia Banci [Italie] ; Francesca Camponeschi [Italie] ; Simone Ciofi-Baffoni [Italie] ; Riccardo Muzzioli [Italie]Source :
- Journal of the American Chemical Society [ 1520-5126 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Protéines de transport, Protéines et peptides de signalisation intracellulaire.
- physiologie : Protéines.
- Humains.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Carrier Proteins, Intracellular Signaling Peptides and Proteins.
- chemical , physiology : Proteins.
- Humans.
Abstract
In eukaryotes, the interaction between members of the monothiol glutaredoxin family and members of the BolA-like protein family has been involved in iron metabolism. To investigate the still unknown functional role of the interaction between human glutaredoxin-3 (GRX3) and its protein partner BOLA2, we characterized at the atomic level the interaction of apo BOLA2 with the apo and holo states of GRX3 and studied the role of BOLA2 in the GRX3-dependent anamorsin maturation pathway. From these studies, it emerged that apo GRX3 and apo BOLA2 form a heterotrimeric complex, composed by two BOLA2 molecules and one GRX3 molecule. This complex is able to bind two [2Fe-2S](2+) clusters, each being bridged between a BOLA2 molecule and a monothiol glutaredoxin domain of GRX3, and to transfer both [2Fe-2S](2+) clusters to apo anamorsin producing its mature holo state. Collectively, the data suggest that the heterotrimeric complex can work as a [2Fe-2S](2+) cluster transfer component in cytosolic Fe/S protein maturation pathways.
DOI: 10.1021/jacs.5b10592
PubMed: 26613676
Affiliations:
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last="Banci">Lucia Banci</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation></author><author><name sortKey="Camponeschi, Francesca" sort="Camponeschi, Francesca" uniqKey="Camponeschi F" first="Francesca" last="Camponeschi">Francesca Camponeschi</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>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 , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation></author><author><name sortKey="Muzzioli, Riccardo" sort="Muzzioli, Riccardo" uniqKey="Muzzioli R" first="Riccardo" last="Muzzioli">Riccardo Muzzioli</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence</wicri:regionArea><wicri:noRegion>Florence</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="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carrier Proteins (metabolism)</term><term>Humans (MeSH)</term><term>Intracellular Signaling Peptides and Proteins (metabolism)</term><term>Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Humains (MeSH)</term><term>Protéines (physiologie)</term><term>Protéines de transport (métabolisme)</term><term>Protéines et peptides de signalisation intracellulaire (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term><term>Intracellular Signaling Peptides and Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de transport</term><term>Protéines et peptides de signalisation intracellulaire</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In eukaryotes, the interaction between members of the monothiol glutaredoxin family and members of the BolA-like protein family has been involved in iron metabolism. To investigate the still unknown functional role of the interaction between human glutaredoxin-3 (GRX3) and its protein partner BOLA2, we characterized at the atomic level the interaction of apo BOLA2 with the apo and holo states of GRX3 and studied the role of BOLA2 in the GRX3-dependent anamorsin maturation pathway. From these studies, it emerged that apo GRX3 and apo BOLA2 form a heterotrimeric complex, composed by two BOLA2 molecules and one GRX3 molecule. This complex is able to bind two [2Fe-2S](2+) clusters, each being bridged between a BOLA2 molecule and a monothiol glutaredoxin domain of GRX3, and to transfer both [2Fe-2S](2+) clusters to apo anamorsin producing its mature holo state. Collectively, the data suggest that the heterotrimeric complex can work as a [2Fe-2S](2+) cluster transfer component in cytosolic Fe/S protein maturation pathways. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26613676</PMID><DateCompleted><Year>2016</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5126</ISSN><JournalIssue CitedMedium="Internet"><Volume>137</Volume><Issue>51</Issue><PubDate><Year>2015</Year><Month>Dec</Month><Day>30</Day></PubDate></JournalIssue><Title>Journal of the American Chemical Society</Title><ISOAbbreviation>J Am Chem Soc</ISOAbbreviation></Journal><ArticleTitle>Elucidating the Molecular Function of Human BOLA2 in GRX3-Dependent Anamorsin Maturation Pathway.</ArticleTitle><Pagination><MedlinePgn>16133-43</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jacs.5b10592</ELocationID><Abstract><AbstractText>In eukaryotes, the interaction between members of the monothiol glutaredoxin family and members of the BolA-like protein family has been involved in iron metabolism. To investigate the still unknown functional role of the interaction between human glutaredoxin-3 (GRX3) and its protein partner BOLA2, we characterized at the atomic level the interaction of apo BOLA2 with the apo and holo states of GRX3 and studied the role of BOLA2 in the GRX3-dependent anamorsin maturation pathway. From these studies, it emerged that apo GRX3 and apo BOLA2 form a heterotrimeric complex, composed by two BOLA2 molecules and one GRX3 molecule. This complex is able to bind two [2Fe-2S](2+) clusters, each being bridged between a BOLA2 molecule and a monothiol glutaredoxin domain of GRX3, and to transfer both [2Fe-2S](2+) clusters to apo anamorsin producing its mature holo state. Collectively, the data suggest that the heterotrimeric complex can work as a [2Fe-2S](2+) cluster transfer component in cytosolic Fe/S protein maturation pathways. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Banci</LastName><ForeName>Lucia</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Camponeschi</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ciofi-Baffoni</LastName><ForeName>Simone</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Muzzioli</LastName><ForeName>Riccardo</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Magnetic Resonance Center CERM, University of Florence , Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Chemistry, University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>12</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Am Chem Soc</MedlineTA><NlmUniqueID>7503056</NlmUniqueID><ISSNLinking>0002-7863</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C533596">BOLA2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C489114">CIAPIN1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C404105">GLRX3 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047908">Intracellular Signaling Peptides and Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047908" MajorTopicYN="N">Intracellular Signaling Peptides and Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>11</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>11</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26613676</ArticleId><ArticleId IdType="doi">10.1021/jacs.5b10592</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name></noRegion><name sortKey="Banci, Lucia" sort="Banci, Lucia" uniqKey="Banci L" first="Lucia" last="Banci">Lucia Banci</name><name sortKey="Camponeschi, Francesca" sort="Camponeschi, Francesca" uniqKey="Camponeschi F" first="Francesca" last="Camponeschi">Francesca Camponeschi</name><name sortKey="Camponeschi, Francesca" sort="Camponeschi, Francesca" uniqKey="Camponeschi F" first="Francesca" last="Camponeschi">Francesca Camponeschi</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="Muzzioli, Riccardo" sort="Muzzioli, Riccardo" uniqKey="Muzzioli R" first="Riccardo" last="Muzzioli">Riccardo Muzzioli</name><name sortKey="Muzzioli, Riccardo" sort="Muzzioli, Riccardo" uniqKey="Muzzioli R" first="Riccardo" 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