IronSulferCluV1, Main, Exploration, bibRecord, 000012

The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins.

Identifieur interne : 000012 ( Main/Exploration ); précédent : 000011; suivant : 000013

The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins.

Auteurs : Mélanie Roland [France] ; Jonathan Przybyla-Toscano [France] ; Florence Vignols [France] ; Nathalie Berger [France] ; Tamanna Azam [États-Unis] ; Loick Christ [France] ; Véronique Santoni [France] ; Hui-Chen Wu [France] ; Tiphaine Dhalleine [France] ; Michael K. Johnson [États-Unis] ; Christian Dubos [France] ; Jérémy Couturier [France] ; Nicolas Rouhier [France]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2020.

RBID : pubmed:31911438

Descripteurs français

English descriptors

KwdEn :
- Arabidopsis (metabolism), Arabidopsis Proteins (metabolism), Chloroplast Proteins (metabolism), Iron-Sulfur Proteins (metabolism), Photosystem I Protein Complex (metabolism), Plastids (metabolism), Protein Binding (MeSH), Protein Interaction Maps (MeSH).
MESH :
- chemical , metabolism : Arabidopsis Proteins, Chloroplast Proteins, Iron-Sulfur Proteins, Photosystem I Protein Complex.
- metabolism : Arabidopsis, Plastids.
- Protein Binding, Protein Interaction Maps.

Abstract

Proteins incorporating iron-sulfur (Fe-S) co-factors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries in plants, located in the cytosol, mitochondria, and chloroplasts. After de novo formation on scaffold proteins, transfer proteins load Fe-S clusters onto client proteins. Among the plastidial representatives of these transfer proteins, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters present in photosystem I subunits, acting upstream of the high-chlorophyll fluorescence 101 (HCF101) protein. NFU2 is also required for the maturation of the [2Fe-2S]-containing dihydroxyacid dehydratase, important for branched-chain amino acid synthesis. Here, we report that recombinant Arabidopsis thaliana NFU1 assembles one [4Fe-4S] cluster per homodimer. Performing co-immunoprecipitation experiments and assessing physical interactions of NFU1 with many [4Fe-4S]-containing plastidial proteins in binary yeast two-hybrid assays, we also gained insights into the specificity of NFU1 for the maturation of chloroplastic Fe-S proteins. Using bimolecular fluorescence complementation and in vitro Fe-S cluster transfer experiments, we confirmed interactions with two proteins involved in isoprenoid and thiamine biosynthesis, 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate synthase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase, respectively. An additional interaction detected with the scaffold protein SUFD enabled us to build a model in which NFU1 receives its Fe-S cluster from the SUFBC₂D scaffold complex and serves in the maturation of specific [4Fe-4S] client proteins. The identification of the NFU1 partner proteins reported here more clearly defines the role of NFU1 in Fe-S client protein maturation in Arabidopsis chloroplasts among other SUF components.

DOI: 10.1074/jbc.RA119.011034
PubMed: 31911438
PubMed Central: PMC7008376

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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 NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins.</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">The plastidial <i>Arabidopsis thaliana</i>
 NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins.</title>
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<author><name sortKey="Azam, Tamanna" sort="Azam, Tamanna" uniqKey="Azam T" first="Tamanna" last="Azam">Tamanna Azam</name>
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<author><name sortKey="Christ, Loick" sort="Christ, Loick" uniqKey="Christ L" first="Loick" last="Christ">Loick Christ</name>
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<country xml:lang="fr">France</country>
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<region type="old region" nuts="2">Lorraine (région)</region>
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<author><name sortKey="Santoni, Veronique" sort="Santoni, Veronique" uniqKey="Santoni V" first="Véronique" last="Santoni">Véronique Santoni</name>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Wu, Hui Chen" sort="Wu, Hui Chen" uniqKey="Wu H" first="Hui-Chen" last="Wu">Hui-Chen Wu</name>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
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<author><name sortKey="Dubos, Christian" sort="Dubos, Christian" uniqKey="Dubos C" first="Christian" last="Dubos">Christian Dubos</name>
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<country xml:lang="fr">France</country>
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<region type="old region">Languedoc-Roussillon</region>
<settlement type="city">Montpellier</settlement>
</placeName>
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<series><title level="j">The Journal of biological chemistry</title>
<idno type="eISSN">1083-351X</idno>
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<term>Arabidopsis Proteins (metabolism)</term>
<term>Chloroplast Proteins (metabolism)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Photosystem I Protein Complex (metabolism)</term>
<term>Plastids (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Interaction Maps (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (métabolisme)</term>
<term>Cartes d'interactions protéiques (MeSH)</term>
<term>Complexe protéique du photosystème I (métabolisme)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Plastes (métabolisme)</term>
<term>Protéines chloroplastiques (métabolisme)</term>
<term>Protéines d'Arabidopsis (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term>
<term>Chloroplast Proteins</term>
<term>Iron-Sulfur Proteins</term>
<term>Photosystem I Protein Complex</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term>
<term>Plastids</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term>
<term>Complexe protéique du photosystème I</term>
<term>Ferrosulfoprotéines</term>
<term>Plastes</term>
<term>Protéines chloroplastiques</term>
<term>Protéines d'Arabidopsis</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Protein Binding</term>
<term>Protein Interaction Maps</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cartes d'interactions protéiques</term>
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<front><div type="abstract" xml:lang="en">Proteins incorporating iron-sulfur (Fe-S) co-factors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries in plants, located in the cytosol, mitochondria, and chloroplasts. After <i>de novo</i>
 formation on scaffold proteins, transfer proteins load Fe-S clusters onto client proteins. Among the plastidial representatives of these transfer proteins, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters present in photosystem I subunits, acting upstream of the high-chlorophyll fluorescence 101 (HCF101) protein. NFU2 is also required for the maturation of the [2Fe-2S]-containing dihydroxyacid dehydratase, important for branched-chain amino acid synthesis. Here, we report that recombinant <i>Arabidopsis thaliana</i>
 NFU1 assembles one [4Fe-4S] cluster per homodimer. Performing co-immunoprecipitation experiments and assessing physical interactions of NFU1 with many [4Fe-4S]-containing plastidial proteins in binary yeast two-hybrid assays, we also gained insights into the specificity of NFU1 for the maturation of chloroplastic Fe-S proteins. Using bimolecular fluorescence complementation and <i>in vitro</i>
 Fe-S cluster transfer experiments, we confirmed interactions with two proteins involved in isoprenoid and thiamine biosynthesis, 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate synthase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase, respectively. An additional interaction detected with the scaffold protein SUFD enabled us to build a model in which NFU1 receives its Fe-S cluster from the SUFBC<sub>2</sub>
D scaffold complex and serves in the maturation of specific [4Fe-4S] client proteins. The identification of the NFU1 partner proteins reported here more clearly defines the role of NFU1 in Fe-S client protein maturation in <i>Arabidopsis</i>
 chloroplasts among other SUF components.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31911438</PMID>
<DateCompleted><Year>2020</Year>
<Month>10</Month>
<Day>14</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>10</Month>
<Day>14</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>295</Volume>
<Issue>6</Issue>
<PubDate><Year>2020</Year>
<Month>02</Month>
<Day>07</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>The plastidial <i>Arabidopsis thaliana</i>
 NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins.</ArticleTitle>
<Pagination><MedlinePgn>1727-1742</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA119.011034</ELocationID>
<Abstract><AbstractText>Proteins incorporating iron-sulfur (Fe-S) co-factors are required for a plethora of metabolic processes. Their maturation depends on three Fe-S cluster assembly machineries in plants, located in the cytosol, mitochondria, and chloroplasts. After <i>de novo</i>
 formation on scaffold proteins, transfer proteins load Fe-S clusters onto client proteins. Among the plastidial representatives of these transfer proteins, NFU2 and NFU3 are required for the maturation of the [4Fe-4S] clusters present in photosystem I subunits, acting upstream of the high-chlorophyll fluorescence 101 (HCF101) protein. NFU2 is also required for the maturation of the [2Fe-2S]-containing dihydroxyacid dehydratase, important for branched-chain amino acid synthesis. Here, we report that recombinant <i>Arabidopsis thaliana</i>
 NFU1 assembles one [4Fe-4S] cluster per homodimer. Performing co-immunoprecipitation experiments and assessing physical interactions of NFU1 with many [4Fe-4S]-containing plastidial proteins in binary yeast two-hybrid assays, we also gained insights into the specificity of NFU1 for the maturation of chloroplastic Fe-S proteins. Using bimolecular fluorescence complementation and <i>in vitro</i>
 Fe-S cluster transfer experiments, we confirmed interactions with two proteins involved in isoprenoid and thiamine biosynthesis, 1-hydroxy-2-methyl-2-(E)-butenyl-4-diphosphate synthase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase, respectively. An additional interaction detected with the scaffold protein SUFD enabled us to build a model in which NFU1 receives its Fe-S cluster from the SUFBC<sub>2</sub>
D scaffold complex and serves in the maturation of specific [4Fe-4S] client proteins. The identification of the NFU1 partner proteins reported here more clearly defines the role of NFU1 in Fe-S client protein maturation in <i>Arabidopsis</i>
 chloroplasts among other SUF components.</AbstractText>
<CopyrightInformation>© 2020 Roland et al.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Roland</LastName>
<ForeName>Mélanie</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Przybyla-Toscano</LastName>
<ForeName>Jonathan</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Vignols</LastName>
<ForeName>Florence</ForeName>
<Initials>F</Initials>
<Identifier Source="ORCID">0000-0002-2031-0407</Identifier>
<AffiliationInfo><Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Berger</LastName>
<ForeName>Nathalie</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Azam</LastName>
<ForeName>Tamanna</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Christ</LastName>
<ForeName>Loick</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Santoni</LastName>
<ForeName>Véronique</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wu</LastName>
<ForeName>Hui-Chen</ForeName>
<Initials>HC</Initials>
<AffiliationInfo><Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dhalleine</LastName>
<ForeName>Tiphaine</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Michael K</ForeName>
<Initials>MK</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dubos</LastName>
<ForeName>Christian</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Couturier</LastName>
<ForeName>Jérémy</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rouhier</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
<Identifier Source="ORCID">0000-0002-2036-7884</Identifier>
<AffiliationInfo><Affiliation>Université de Lorraine, INRAE, IAM, F-54000 Nancy, France nicolas.rouhier@univ-lorraine.fr.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R37 GM062524</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2020</Year>
<Month>01</Month>
<Day>06</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C000709550">AT4G01940 protein, Arabidopsis</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060365" MajorTopicYN="N">Chloroplast Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045331" MajorTopicYN="N">Photosystem I Protein Complex</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018087" MajorTopicYN="N">Plastids</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060066" MajorTopicYN="Y">Protein Interaction Maps</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Arabidopsis thaliana</Keyword>
<Keyword MajorTopicYN="Y">NFU</Keyword>
<Keyword MajorTopicYN="Y">chloroplast</Keyword>
<Keyword MajorTopicYN="Y">iron–sulfur protein</Keyword>
<Keyword MajorTopicYN="Y">maturation</Keyword>
<Keyword MajorTopicYN="Y">protein assembly</Keyword>
<Keyword MajorTopicYN="Y">sulfur</Keyword>
</KeywordList>
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<Reference><Citation>Mol Biol Cell. 2012 Apr;23(7):1157-66</Citation>
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<settlement><li>Montpellier</li>
<li>Nancy</li>
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<orgName><li>Université de Lorraine</li>
</orgName>
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<tree><country name="France"><region name="Grand Est"><name sortKey="Roland, Melanie" sort="Roland, Melanie" uniqKey="Roland M" first="Mélanie" last="Roland">Mélanie Roland</name>
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<name sortKey="Berger, Nathalie" sort="Berger, Nathalie" uniqKey="Berger N" first="Nathalie" last="Berger">Nathalie Berger</name>
<name sortKey="Christ, Loick" sort="Christ, Loick" uniqKey="Christ L" first="Loick" last="Christ">Loick Christ</name>
<name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name>
<name sortKey="Dhalleine, Tiphaine" sort="Dhalleine, Tiphaine" uniqKey="Dhalleine T" first="Tiphaine" last="Dhalleine">Tiphaine Dhalleine</name>
<name sortKey="Dubos, Christian" sort="Dubos, Christian" uniqKey="Dubos C" first="Christian" last="Dubos">Christian Dubos</name>
<name sortKey="Przybyla Toscano, Jonathan" sort="Przybyla Toscano, Jonathan" uniqKey="Przybyla Toscano J" first="Jonathan" last="Przybyla-Toscano">Jonathan Przybyla-Toscano</name>
<name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
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<name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</name>
<name sortKey="Wu, Hui Chen" sort="Wu, Hui Chen" uniqKey="Wu H" first="Hui-Chen" last="Wu">Hui-Chen Wu</name>
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<country name="États-Unis"><region name="Géorgie (États-Unis)"><name sortKey="Azam, Tamanna" sort="Azam, Tamanna" uniqKey="Azam T" first="Tamanna" last="Azam">Tamanna Azam</name>
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<name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
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The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins.

The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins.

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