The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea.
Identifieur interne : 000024 ( Main/Exploration ); précédent : 000023; suivant : 000025The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea.
Auteurs : Cuiping Zhao [États-Unis] ; Zhe Lyu [États-Unis] ; Feng Long [États-Unis] ; Taiwo Akinyemi [États-Unis] ; Kasidet Manakongtreecheep [États-Unis] ; Dieter Söll [États-Unis] ; William B. Whitman [États-Unis] ; David J. Vinyard [États-Unis] ; Yuchen Liu [États-Unis]Source :
- FEBS letters [ 1873-3468 ] ; 2020.
Descripteurs français
- KwdFr :
- Cytosol (métabolisme), Délétion de gène (MeSH), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Methanococcus (croissance et développement), Methanococcus (génétique), Methanococcus (métabolisme), Noyau de la cellule (métabolisme), Phylogenèse (MeSH), Protéines d'archée (génétique), Protéines d'archée (métabolisme).
- MESH :
- croissance et développement : Methanococcus.
- génétique : Ferrosulfoprotéines, Methanococcus, Protéines d'archée.
- métabolisme : Cytosol, Ferrosulfoprotéines, Methanococcus, Noyau de la cellule, Protéines d'archée.
- Délétion de gène, Phylogenèse.
English descriptors
- KwdEn :
- Archaeal Proteins (genetics), Archaeal Proteins (metabolism), Cell Nucleus (metabolism), Cytosol (metabolism), Gene Deletion (MeSH), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Methanococcus (genetics), Methanococcus (growth & development), Methanococcus (metabolism), Phylogeny (MeSH).
- MESH :
- chemical , genetics : Archaeal Proteins, Iron-Sulfur Proteins.
- chemical , metabolism : Archaeal Proteins, Iron-Sulfur Proteins.
- genetics : Methanococcus.
- growth & development : Methanococcus.
- metabolism : Cell Nucleus, Cytosol, Methanococcus.
- Gene Deletion, Phylogeny.
Abstract
The nucleotide binding protein 35 (Nbp35)/cytosolic Fe-S cluster deficient 1 (Cfd1)/alternative pyrimidine biosynthetic protein C (ApbC) protein homologs have been identified in all three domains of life. In eukaryotes, the Nbp35/Cfd1 heterocomplex is an essential Fe-S cluster assembly scaffold required for the maturation of Fe-S proteins in the cytosol and nucleus, whereas the bacterial ApbC is an Fe-S cluster transfer protein only involved in the maturation of a specific target protein. Here, we show that the Nbp35/ApbC homolog MMP0704 purified from its native archaeal host Methanococcus maripaludis contains a [4Fe-4S] cluster that can be transferred to a [4Fe-4S] apoprotein. Deletion of mmp0704 from M. maripaludis does not cause growth deficiency under our tested conditions. Our data indicate that Nbp35/ApbC is a nonessential [4Fe-4S] cluster transfer protein in methanogenic archaea.
DOI: 10.1002/1873-3468.13673
PubMed: 31709520
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea.</title>
<author><name sortKey="Zhao, Cuiping" sort="Zhao, Cuiping" uniqKey="Zhao C" first="Cuiping" last="Zhao">Cuiping Zhao</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA</wicri:regionArea>
<placeName><region type="state">Louisiane</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Lyu, Zhe" sort="Lyu, Zhe" uniqKey="Lyu Z" first="Zhe" last="Lyu">Zhe Lyu</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Long, Feng" sort="Long, Feng" uniqKey="Long F" first="Feng" last="Long">Feng Long</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Akinyemi, Taiwo" sort="Akinyemi, Taiwo" uniqKey="Akinyemi T" first="Taiwo" last="Akinyemi">Taiwo Akinyemi</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Manakongtreecheep, Kasidet" sort="Manakongtreecheep, Kasidet" uniqKey="Manakongtreecheep K" first="Kasidet" last="Manakongtreecheep">Kasidet Manakongtreecheep</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT</wicri:regionArea>
<placeName><region type="state">Connecticut</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Soll, Dieter" sort="Soll, Dieter" uniqKey="Soll D" first="Dieter" last="Söll">Dieter Söll</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT</wicri:regionArea>
<placeName><region type="state">Connecticut</region>
</placeName>
</affiliation>
<affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry, Yale University, New Haven, CT, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Chemistry, Yale University, New Haven, CT</wicri:regionArea>
<placeName><region type="state">Connecticut</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Whitman, William B" sort="Whitman, William B" uniqKey="Whitman W" first="William B" last="Whitman">William B. Whitman</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Vinyard, David J" sort="Vinyard, David J" uniqKey="Vinyard D" first="David J" last="Vinyard">David J. Vinyard</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA</wicri:regionArea>
<placeName><region type="state">Louisiane</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Liu, Yuchen" sort="Liu, Yuchen" uniqKey="Liu Y" first="Yuchen" last="Liu">Yuchen Liu</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA</wicri:regionArea>
<placeName><region type="state">Louisiane</region>
</placeName>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2020">2020</date>
<idno type="RBID">pubmed:31709520</idno>
<idno type="pmid">31709520</idno>
<idno type="doi">10.1002/1873-3468.13673</idno>
<idno type="wicri:Area/Main/Corpus">000203</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000203</idno>
<idno type="wicri:Area/Main/Curation">000203</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000203</idno>
<idno type="wicri:Area/Main/Exploration">000203</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea.</title>
<author><name sortKey="Zhao, Cuiping" sort="Zhao, Cuiping" uniqKey="Zhao C" first="Cuiping" last="Zhao">Cuiping Zhao</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA</wicri:regionArea>
<placeName><region type="state">Louisiane</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Lyu, Zhe" sort="Lyu, Zhe" uniqKey="Lyu Z" first="Zhe" last="Lyu">Zhe Lyu</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Long, Feng" sort="Long, Feng" uniqKey="Long F" first="Feng" last="Long">Feng Long</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Akinyemi, Taiwo" sort="Akinyemi, Taiwo" uniqKey="Akinyemi T" first="Taiwo" last="Akinyemi">Taiwo Akinyemi</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Manakongtreecheep, Kasidet" sort="Manakongtreecheep, Kasidet" uniqKey="Manakongtreecheep K" first="Kasidet" last="Manakongtreecheep">Kasidet Manakongtreecheep</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT</wicri:regionArea>
<placeName><region type="state">Connecticut</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Soll, Dieter" sort="Soll, Dieter" uniqKey="Soll D" first="Dieter" last="Söll">Dieter Söll</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT</wicri:regionArea>
<placeName><region type="state">Connecticut</region>
</placeName>
</affiliation>
<affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry, Yale University, New Haven, CT, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Chemistry, Yale University, New Haven, CT</wicri:regionArea>
<placeName><region type="state">Connecticut</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Whitman, William B" sort="Whitman, William B" uniqKey="Whitman W" first="William B" last="Whitman">William B. Whitman</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology, University of Georgia, Athens, GA</wicri:regionArea>
<placeName><region type="state">Géorgie (États-Unis)</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Vinyard, David J" sort="Vinyard, David J" uniqKey="Vinyard D" first="David J" last="Vinyard">David J. Vinyard</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA</wicri:regionArea>
<placeName><region type="state">Louisiane</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Liu, Yuchen" sort="Liu, Yuchen" uniqKey="Liu Y" first="Yuchen" last="Liu">Yuchen Liu</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA</wicri:regionArea>
<placeName><region type="state">Louisiane</region>
</placeName>
</affiliation>
</author>
</analytic>
<series><title level="j">FEBS letters</title>
<idno type="eISSN">1873-3468</idno>
<imprint><date when="2020" type="published">2020</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Archaeal Proteins (genetics)</term>
<term>Archaeal Proteins (metabolism)</term>
<term>Cell Nucleus (metabolism)</term>
<term>Cytosol (metabolism)</term>
<term>Gene Deletion (MeSH)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Methanococcus (genetics)</term>
<term>Methanococcus (growth & development)</term>
<term>Methanococcus (metabolism)</term>
<term>Phylogeny (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cytosol (métabolisme)</term>
<term>Délétion de gène (MeSH)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Methanococcus (croissance et développement)</term>
<term>Methanococcus (génétique)</term>
<term>Methanococcus (métabolisme)</term>
<term>Noyau de la cellule (métabolisme)</term>
<term>Phylogenèse (MeSH)</term>
<term>Protéines d'archée (génétique)</term>
<term>Protéines d'archée (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Archaeal Proteins</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Archaeal Proteins</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Methanococcus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Methanococcus</term>
</keywords>
<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Methanococcus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferrosulfoprotéines</term>
<term>Methanococcus</term>
<term>Protéines d'archée</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term>
<term>Cytosol</term>
<term>Methanococcus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosol</term>
<term>Ferrosulfoprotéines</term>
<term>Methanococcus</term>
<term>Noyau de la cellule</term>
<term>Protéines d'archée</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Gene Deletion</term>
<term>Phylogeny</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Délétion de gène</term>
<term>Phylogenèse</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The nucleotide binding protein 35 (Nbp35)/cytosolic Fe-S cluster deficient 1 (Cfd1)/alternative pyrimidine biosynthetic protein C (ApbC) protein homologs have been identified in all three domains of life. In eukaryotes, the Nbp35/Cfd1 heterocomplex is an essential Fe-S cluster assembly scaffold required for the maturation of Fe-S proteins in the cytosol and nucleus, whereas the bacterial ApbC is an Fe-S cluster transfer protein only involved in the maturation of a specific target protein. Here, we show that the Nbp35/ApbC homolog MMP0704 purified from its native archaeal host Methanococcus maripaludis contains a [4Fe-4S] cluster that can be transferred to a [4Fe-4S] apoprotein. Deletion of mmp0704 from M. maripaludis does not cause growth deficiency under our tested conditions. Our data indicate that Nbp35/ApbC is a nonessential [4Fe-4S] cluster transfer protein in methanogenic archaea.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31709520</PMID>
<DateCompleted><Year>2020</Year>
<Month>10</Month>
<Day>05</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>10</Month>
<Day>05</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>594</Volume>
<Issue>5</Issue>
<PubDate><Year>2020</Year>
<Month>03</Month>
</PubDate>
</JournalIssue>
<Title>FEBS letters</Title>
<ISOAbbreviation>FEBS Lett</ISOAbbreviation>
</Journal>
<ArticleTitle>The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea.</ArticleTitle>
<Pagination><MedlinePgn>924-932</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1002/1873-3468.13673</ELocationID>
<Abstract><AbstractText>The nucleotide binding protein 35 (Nbp35)/cytosolic Fe-S cluster deficient 1 (Cfd1)/alternative pyrimidine biosynthetic protein C (ApbC) protein homologs have been identified in all three domains of life. In eukaryotes, the Nbp35/Cfd1 heterocomplex is an essential Fe-S cluster assembly scaffold required for the maturation of Fe-S proteins in the cytosol and nucleus, whereas the bacterial ApbC is an Fe-S cluster transfer protein only involved in the maturation of a specific target protein. Here, we show that the Nbp35/ApbC homolog MMP0704 purified from its native archaeal host Methanococcus maripaludis contains a [4Fe-4S] cluster that can be transferred to a [4Fe-4S] apoprotein. Deletion of mmp0704 from M. maripaludis does not cause growth deficiency under our tested conditions. Our data indicate that Nbp35/ApbC is a nonessential [4Fe-4S] cluster transfer protein in methanogenic archaea.</AbstractText>
<CopyrightInformation>© 2019 Federation of European Biochemical Societies.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhao</LastName>
<ForeName>Cuiping</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lyu</LastName>
<ForeName>Zhe</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Long</LastName>
<ForeName>Feng</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Akinyemi</LastName>
<ForeName>Taiwo</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Manakongtreecheep</LastName>
<ForeName>Kasidet</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Söll</LastName>
<ForeName>Dieter</ForeName>
<Initials>D</Initials>
<Identifier Source="ORCID">0000-0002-3077-8986</Identifier>
<AffiliationInfo><Affiliation>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Chemistry, Yale University, New Haven, CT, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Whitman</LastName>
<ForeName>William B</ForeName>
<Initials>WB</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, University of Georgia, Athens, GA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Vinyard</LastName>
<ForeName>David J</ForeName>
<Initials>DJ</Initials>
<AffiliationInfo><Affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Yuchen</ForeName>
<Initials>Y</Initials>
<Identifier Source="ORCID">0000-0003-0842-5882</Identifier>
<AffiliationInfo><Affiliation>Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA.</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>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>11</Month>
<Day>27</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>FEBS Lett</MedlineTA>
<NlmUniqueID>0155157</NlmUniqueID>
<ISSNLinking>0014-5793</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D019843">Archaeal Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D019843" MajorTopicYN="N">Archaeal Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017017" MajorTopicYN="N">Methanococcus</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Methanococcus maripaludis
</Keyword>
<Keyword MajorTopicYN="Y">ApbC</Keyword>
<Keyword MajorTopicYN="Y">Nbp35</Keyword>
<Keyword MajorTopicYN="Y">archaea</Keyword>
<Keyword MajorTopicYN="Y">iron-sulfur cluster</Keyword>
<Keyword MajorTopicYN="Y">methanogen</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year>
<Month>06</Month>
<Day>18</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2019</Year>
<Month>11</Month>
<Day>04</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2019</Year>
<Month>11</Month>
<Day>05</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2019</Year>
<Month>11</Month>
<Day>12</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2020</Year>
<Month>10</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2019</Year>
<Month>11</Month>
<Day>12</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">31709520</ArticleId>
<ArticleId IdType="doi">10.1002/1873-3468.13673</ArticleId>
</ArticleIdList>
<ReferenceList><Title>References</Title>
<Reference><Citation>Johnson DC, Dean DR, Smith AD and Johnson MK (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74, 247-281.</Citation>
</Reference>
<Reference><Citation>Meyer J (2008) Iron-sulfur protein folds, iron-sulfur chemistry, and evolution. J Biol Inorg Chem 13, 157-170.</Citation>
</Reference>
<Reference><Citation>Pain D and Dancis A (2016) Roles of Fe-S proteins: from cofactor synthesis to iron homeostasis to protein synthesis. Curr Opin Genet Dev 38, 45-51.</Citation>
</Reference>
<Reference><Citation>Lill R (2009) Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838.</Citation>
</Reference>
<Reference><Citation>Py B and Barras F (2010) Building Fe-S proteins: bacterial strategies. Nat Rev Microbiol 8, 436-446.</Citation>
</Reference>
<Reference><Citation>Zheng L, White RH, Cash VL, Jack RF and Dean DR (1993) Cysteine desulfurase activity indicates a role for NifS in metallocluster biosynthesis. Proc Natl Acad Sci USA 90, 2754-2758.</Citation>
</Reference>
<Reference><Citation>Blanc B, Gerez C and Ollagnier de Choudens S (2015) Assembly of Fe/S proteins in bacterial systems: biochemistry of the bacterial ISC system. Biochim Biophys Acta 1853, 1436-1447.</Citation>
</Reference>
<Reference><Citation>Raulfs EC, O'Carroll IP, Dos Santos PC, Unciuleac MC and Dean DR (2008) In vivo iron-sulfur cluster formation. Proc Natl Acad Sci USA 105, 8591-8596.</Citation>
</Reference>
<Reference><Citation>Yuvaniyama P, Agar JN, Cash VL, Johnson MK and Dean DR (2000) NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein. Proc Natl Acad Sci USA 97, 599-604.</Citation>
</Reference>
<Reference><Citation>Outten FW (2015) Recent advances in the Suf Fe-S cluster biogenesis pathway: beyond the proteobacteria. Biochim Biophys Acta 1853, 1464-1469.</Citation>
</Reference>
<Reference><Citation>Roche B, Aussel L, Ezraty B, Mandin P, Py B and Barras F (2013) Iron/sulfur proteins biogenesis in prokaryotes: formation, regulation and diversity. Biochim Biophys Acta 1827, 455-469.</Citation>
</Reference>
<Reference><Citation>Braymer JJ and Lill R (2017) Iron-sulfur cluster biogenesis and trafficking in mitochondria. J Biol Chem 292, 12754-12763.</Citation>
</Reference>
<Reference><Citation>Lu Y (2018) Assembly and transfer of iron-sulfur clusters in the plastid. Front Plant Sci 9, 336.</Citation>
</Reference>
<Reference><Citation>Netz DJ, Mascarenhas J, Stehling O, Pierik AJ and Lill R (2014) Maturation of cytosolic and nuclear iron-sulfur proteins. Trends Cell Biol 24, 303-312.</Citation>
</Reference>
<Reference><Citation>Grossman JD, Camire EJ and Perlstein DL (2018) Approaches to interrogate the role of nucleotide hydrolysis by metal trafficking NTPases: the Nbp35-Cfd1 iron-sulfur cluster scaffold as a case study. Methods Enzymol 599, 293-325.</Citation>
</Reference>
<Reference><Citation>Hausmann A, Aguilar Netz DJ, Balk J, Pierik AJ, Muhlenhoff U and Lill R (2005) The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Proc Natl Acad Sci USA 102, 3266-3271.</Citation>
</Reference>
<Reference><Citation>Netz DJ, Pierik AJ, Stumpfig M, Muhlenhoff U and Lill R (2007) The Cfd1-Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nat Chem Biol 3, 278-286.</Citation>
</Reference>
<Reference><Citation>Stehling O, Netz DJ, Niggemeyer B, Rösser R, Eisenstein RS, Puccio H, Pierik AJ and Lill R (2008) Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis. Mol Cell Biol 28, 5517-5528.</Citation>
</Reference>
<Reference><Citation>Netz DJ, Pierik AJ, Stumpfig M, Bill E, Sharma AK, Pallesen LJ, Walden WE and Lill R (2012) A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation. J Biol Chem 287, 12365-12378.</Citation>
</Reference>
<Reference><Citation>Pallesen LJ, Solodovnikova N, Sharma AK and Walden WE (2013) Interaction with Cfd1 increases the kinetic lability of FeS on the Nbp35 scaffold. J Biol Chem 288, 23358-23367.</Citation>
</Reference>
<Reference><Citation>Camire EJ, Grossman JD, Thole GJ, Fleischman NM and Perlstein DL (2015) The yeast Nbp35-Cfd1 cytosolic iron-sulfur cluster scaffold is an ATPase. J Biol Chem 290, 23793-23802.</Citation>
</Reference>
<Reference><Citation>Grossman JD, Gay KA, Camire EJ, Walden WE and Perlstein DL (2019) Coupling nucleotide binding and hydrolysis to iron-sulfur cluster acquisition and transfer revealed through genetic dissection of the Nbp35 ATPase site. Biochemistry 58, 2017-2027.</Citation>
</Reference>
<Reference><Citation>Boyd JM, Pierik AJ, Netz DJ, Lill R and Downs DM (2008) Bacterial ApbC can bind and effectively transfer iron-sulfur clusters. Biochemistry 47, 8195-8202.</Citation>
</Reference>
<Reference><Citation>Boyd JM, Sondelski JL and Downs DM (2009) Bacterial ApbC protein has two biochemical activities that are required for in vivo function. J Biol Chem 284, 110-8.</Citation>
</Reference>
<Reference><Citation>Liu Y, Sieprawska-Lupa M, Whitman WB and White RH (2010) Cysteine is not the sulfur source for iron-sulfur cluster and methionine biosynthesis in the methanogenic archaeon Methanococcus maripaludis. J Biol Chem 285, 31923-31929.</Citation>
</Reference>
<Reference><Citation>Boyd JM, Drevland RM, Downs DM and Graham DE (2009) Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins. J Bacteriol 191, 1490-1497.</Citation>
</Reference>
<Reference><Citation>Whitman WB, Shieh J, Sohn S, Caras DS and Premachandran U (1986) Isolation and characterization of 22 mesophilic methanococci. Syst Appl Microbiol 7, 235-240.</Citation>
</Reference>
<Reference><Citation>Walters AD, Smith SE and Chong JP (2011) Shuttle vector system for Methanococcus maripaludis with improved transformation efficiency. Appl Environ Microbiol 77, 2549-2551.</Citation>
</Reference>
<Reference><Citation>Sarmiento F, Leigh JA and Whitman WB (2011) Genetic systems for hydrogenotrophic methanogens. Methods Enzymol 494, 43-73.</Citation>
</Reference>
<Reference><Citation>Lyu Z, Chou C-w, Shi H, Patel R, Duin EC and Whitman WB (2017) Mmp10 is required for post-translational methylation of arginine at the active site of methyl-coenzyme M reductase. bioRxiv, 211441. “[PREPRINT]”</Citation>
</Reference>
<Reference><Citation>Stoll S and Schweiger A (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J Magn Reson 178, 42-55.</Citation>
</Reference>
<Reference><Citation>Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, Toyonaga H and Mori H (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12, 291-299.</Citation>
</Reference>
<Reference><Citation>Liu Y, Vinyard DJ, Reesbeck ME, Suzuki T, Manakongtreecheep K, Holland PL, Brudvig GW and Söll D (2016) A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes. Proc Natl Acad Sci USA 113, 12703-12708.</Citation>
</Reference>
<Reference><Citation>Gardner P and Fridovich I (1992) Inactivation-reactivation of aconitase in Escherichia coli: a sensitive measure of superoxide radical. J Biol Chem 267, 8757-8763.</Citation>
</Reference>
<Reference><Citation>Kumar S, Stecher G, Li M, Knyaz C and Tamura K (2018) MEGA X: Molecular evolutionary genetics analysis across computing platforms. Mol Biol Evol 35, 1547-1549.</Citation>
</Reference>
<Reference><Citation>Le SQ and Gascuel O (2008) An improved general amino acid replacement matrix. Mol Biol Evol 25, 1307-1320.</Citation>
</Reference>
<Reference><Citation>Felsenstein J (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution Int J Org Evolution 39, 783-791.</Citation>
</Reference>
<Reference><Citation>Liu J, Chakraborty S, Hosseinzadeh P, Yu Y, Tian S, Petrik I, Bhagi A and Lu Y (2014) Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers. Chem Rev 114, 4366-4469.</Citation>
</Reference>
<Reference><Citation>Weil JA and Bolton JR (2007) Basic principles of paramagnetic resonance. In Electron Paramagnetic Resonance: Elementary Theory and Practical Applications (Weil JA and Bolton JR, eds), pp. 1-35. John Wiley & Sons, Inc., Hoboken, NJ.</Citation>
</Reference>
<Reference><Citation>Sarmiento F, Mrázek J and Whitman WB (2013) Genome-scale analysis of gene function in the hydrogenotrophic methanogenic archaeon Methanococcus maripaludis. Proc Natl Acad Sci USA 110, 4726-4731.</Citation>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Connecticut</li>
<li>Géorgie (États-Unis)</li>
<li>Louisiane</li>
</region>
</list>
<tree><country name="États-Unis"><region name="Louisiane"><name sortKey="Zhao, Cuiping" sort="Zhao, Cuiping" uniqKey="Zhao C" first="Cuiping" last="Zhao">Cuiping Zhao</name>
</region>
<name sortKey="Akinyemi, Taiwo" sort="Akinyemi, Taiwo" uniqKey="Akinyemi T" first="Taiwo" last="Akinyemi">Taiwo Akinyemi</name>
<name sortKey="Liu, Yuchen" sort="Liu, Yuchen" uniqKey="Liu Y" first="Yuchen" last="Liu">Yuchen Liu</name>
<name sortKey="Long, Feng" sort="Long, Feng" uniqKey="Long F" first="Feng" last="Long">Feng Long</name>
<name sortKey="Lyu, Zhe" sort="Lyu, Zhe" uniqKey="Lyu Z" first="Zhe" last="Lyu">Zhe Lyu</name>
<name sortKey="Manakongtreecheep, Kasidet" sort="Manakongtreecheep, Kasidet" uniqKey="Manakongtreecheep K" first="Kasidet" last="Manakongtreecheep">Kasidet Manakongtreecheep</name>
<name sortKey="Soll, Dieter" sort="Soll, Dieter" uniqKey="Soll D" first="Dieter" last="Söll">Dieter Söll</name>
<name sortKey="Soll, Dieter" sort="Soll, Dieter" uniqKey="Soll D" first="Dieter" last="Söll">Dieter Söll</name>
<name sortKey="Vinyard, David J" sort="Vinyard, David J" uniqKey="Vinyard D" first="David J" last="Vinyard">David J. Vinyard</name>
<name sortKey="Whitman, William B" sort="Whitman, William B" uniqKey="Whitman W" first="William B" last="Whitman">William B. Whitman</name>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/IronSulferCluV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000024 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000024 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= IronSulferCluV1 |flux= Main |étape= Exploration |type= RBID |clé= pubmed:31709520 |texte= The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:31709520" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \ | NlmPubMed2Wicri -a IronSulferCluV1
This area was generated with Dilib version V0.6.38. |