The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes.
Identifieur interne : 000911 ( Main/Exploration ); précédent : 000910; suivant : 000912The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes.
Auteurs : N. Yeung [États-Unis] ; B. Gold ; N L Liu ; R. Prathapam ; H J Sterling ; E R Willams ; G. ButlandSource :
- Biochemistry [ 1520-4995 ] ; 2011.
Descripteurs français
- KwdFr :
- Chromatographie sur gel (méthodes), Dichroïsme circulaire (méthodes), Dimérisation (MeSH), Escherichia coli (métabolisme), Fer (composition chimique), Ferrosulfoprotéines (composition chimique), Glutarédoxines (composition chimique), Humains (MeSH), Modèles génétiques (MeSH), Mutation (MeSH), Plasmides (métabolisme), Protéines Escherichia coli (composition chimique), Spectrométrie de masse (méthodes), Spectrophotométrie (méthodes), Spectrophotométrie UV (méthodes).
- MESH :
- composition chimique : Fer, Ferrosulfoprotéines, Glutarédoxines, Protéines Escherichia coli.
- métabolisme : Escherichia coli, Plasmides.
- méthodes : Chromatographie sur gel, Dichroïsme circulaire, Spectrométrie de masse, Spectrophotométrie, Spectrophotométrie UV.
- Dimérisation, Humains, Modèles génétiques, Mutation.
English descriptors
- KwdEn :
- Chromatography, Gel (methods), Circular Dichroism (methods), Dimerization (MeSH), Escherichia coli (metabolism), Escherichia coli Proteins (chemistry), Glutaredoxins (chemistry), Humans (MeSH), Iron (chemistry), Iron-Sulfur Proteins (chemistry), Mass Spectrometry (methods), Models, Genetic (MeSH), Mutation (MeSH), Plasmids (metabolism), Spectrophotometry (methods), Spectrophotometry, Ultraviolet (methods).
- MESH :
- chemical , chemistry : Escherichia coli Proteins, Glutaredoxins, Iron, Iron-Sulfur Proteins.
- metabolism : Escherichia coli, Plasmids.
- methods : Chromatography, Gel, Circular Dichroism, Mass Spectrometry, Spectrophotometry, Spectrophotometry, Ultraviolet.
- Dimerization, Humans, Models, Genetic, Mutation.
Abstract
Monothiol glutaredoxins (mono-Grx) represent a highly evolutionarily conserved class of proteins present in organisms ranging from prokaryotes to humans. Mono-Grxs have been implicated in iron sulfur (FeS) cluster biosynthesis as potential scaffold proteins and in iron homeostasis via an FeS-containing complex with Fra2p (homologue of E. coli BolA) in yeast and are linked to signal transduction in mammalian systems. However, the function of the mono-Grx in prokaryotes and the nature of an interaction with BolA-like proteins have not been established. Recent genome-wide screens for E. coli genetic interactions reported the synthetic lethality (combination of mutations leading to cell death; mutation of only one of these genes does not) of a grxD mutation when combined with strains defective in FeS cluster biosynthesis (isc operon) functions [Butland, G., et al. (2008) Nature Methods 5, 789-795]. These data connected the only E. coli mono-Grx, GrxD to a potential role in FeS cluster biosynthesis. We investigated GrxD to uncover the molecular basis of this synthetic lethality and observed that GrxD can form FeS-bound homodimeric and BolA containing heterodimeric complexes. These complexes display substantially different spectroscopic and functional properties, including the ability to act as scaffold proteins for intact FeS cluster transfer to the model [2Fe-2S] acceptor protein E. coli apo-ferredoxin (Fdx), with the homodimer being significantly more efficient. In this work, we functionally dissect the potential cellular roles of GrxD as a component of both homodimeric and heterodimeric complexes to ultimately uncover if either of these complexes performs functions linked to FeS cluster biosynthesis.
DOI: 10.1021/bi2008883
PubMed: 21899261
PubMed Central: PMC3236052
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Butland</name></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Gel (methods)</term><term>Circular Dichroism (methods)</term><term>Dimerization (MeSH)</term><term>Escherichia coli (metabolism)</term><term>Escherichia coli Proteins (chemistry)</term><term>Glutaredoxins (chemistry)</term><term>Humans (MeSH)</term><term>Iron (chemistry)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Mass Spectrometry (methods)</term><term>Models, Genetic (MeSH)</term><term>Mutation (MeSH)</term><term>Plasmids (metabolism)</term><term>Spectrophotometry (methods)</term><term>Spectrophotometry, Ultraviolet (methods)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie sur gel (méthodes)</term><term>Dichroïsme circulaire (méthodes)</term><term>Dimérisation (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Fer (composition chimique)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Glutarédoxines (composition chimique)</term><term>Humains (MeSH)</term><term>Modèles génétiques (MeSH)</term><term>Mutation (MeSH)</term><term>Plasmides (métabolisme)</term><term>Protéines Escherichia coli (composition chimique)</term><term>Spectrométrie de masse (méthodes)</term><term>Spectrophotométrie (méthodes)</term><term>Spectrophotométrie UV (méthodes)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Escherichia coli Proteins</term><term>Glutaredoxins</term><term>Iron</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Fer</term><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Protéines Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Plasmids</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chromatography, Gel</term><term>Circular Dichroism</term><term>Mass Spectrometry</term><term>Spectrophotometry</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Plasmides</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Chromatographie sur gel</term><term>Dichroïsme circulaire</term><term>Spectrométrie de masse</term><term>Spectrophotométrie</term><term>Spectrophotométrie UV</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Dimerization</term><term>Humans</term><term>Models, Genetic</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dimérisation</term><term>Humains</term><term>Modèles génétiques</term><term>Mutation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Monothiol glutaredoxins (mono-Grx) represent a highly evolutionarily conserved class of proteins present in organisms ranging from prokaryotes to humans. Mono-Grxs have been implicated in iron sulfur (FeS) cluster biosynthesis as potential scaffold proteins and in iron homeostasis via an FeS-containing complex with Fra2p (homologue of E. coli BolA) in yeast and are linked to signal transduction in mammalian systems. However, the function of the mono-Grx in prokaryotes and the nature of an interaction with BolA-like proteins have not been established. Recent genome-wide screens for E. coli genetic interactions reported the synthetic lethality (combination of mutations leading to cell death; mutation of only one of these genes does not) of a grxD mutation when combined with strains defective in FeS cluster biosynthesis (isc operon) functions [Butland, G., et al. (2008) Nature Methods 5, 789-795]. These data connected the only E. coli mono-Grx, GrxD to a potential role in FeS cluster biosynthesis. We investigated GrxD to uncover the molecular basis of this synthetic lethality and observed that GrxD can form FeS-bound homodimeric and BolA containing heterodimeric complexes. These complexes display substantially different spectroscopic and functional properties, including the ability to act as scaffold proteins for intact FeS cluster transfer to the model [2Fe-2S] acceptor protein E. coli apo-ferredoxin (Fdx), with the homodimer being significantly more efficient. In this work, we functionally dissect the potential cellular roles of GrxD as a component of both homodimeric and heterodimeric complexes to ultimately uncover if either of these complexes performs functions linked to FeS cluster biosynthesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21899261</PMID><DateCompleted><Year>2011</Year><Month>12</Month><Day>20</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>50</Volume><Issue>41</Issue><PubDate><Year>2011</Year><Month>Oct</Month><Day>18</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes.</ArticleTitle><Pagination><MedlinePgn>8957-69</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/bi2008883</ELocationID><Abstract><AbstractText>Monothiol glutaredoxins (mono-Grx) represent a highly evolutionarily conserved class of proteins present in organisms ranging from prokaryotes to humans. Mono-Grxs have been implicated in iron sulfur (FeS) cluster biosynthesis as potential scaffold proteins and in iron homeostasis via an FeS-containing complex with Fra2p (homologue of E. coli BolA) in yeast and are linked to signal transduction in mammalian systems. However, the function of the mono-Grx in prokaryotes and the nature of an interaction with BolA-like proteins have not been established. Recent genome-wide screens for E. coli genetic interactions reported the synthetic lethality (combination of mutations leading to cell death; mutation of only one of these genes does not) of a grxD mutation when combined with strains defective in FeS cluster biosynthesis (isc operon) functions [Butland, G., et al. (2008) Nature Methods 5, 789-795]. These data connected the only E. coli mono-Grx, GrxD to a potential role in FeS cluster biosynthesis. We investigated GrxD to uncover the molecular basis of this synthetic lethality and observed that GrxD can form FeS-bound homodimeric and BolA containing heterodimeric complexes. These complexes display substantially different spectroscopic and functional properties, including the ability to act as scaffold proteins for intact FeS cluster transfer to the model [2Fe-2S] acceptor protein E. coli apo-ferredoxin (Fdx), with the homodimer being significantly more efficient. In this work, we functionally dissect the potential cellular roles of GrxD as a component of both homodimeric and heterodimeric complexes to ultimately uncover if either of these complexes performs functions linked to FeS cluster biosynthesis.</AbstractText><CopyrightInformation>© 2011 American Chemical Society</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yeung</LastName><ForeName>N</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>N L</ForeName><Initials>NL</Initials></Author><Author ValidYN="Y"><LastName>Prathapam</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Sterling</LastName><ForeName>H J</ForeName><Initials>HJ</Initials></Author><Author ValidYN="Y"><LastName>Willams</LastName><ForeName>E R</ForeName><Initials>ER</Initials></Author><Author ValidYN="Y"><LastName>Butland</LastName><ForeName>G</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM088196</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 GM008295</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P30 CA082103</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM088196</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32GM08295</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM088196-02</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><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>09</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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Spectrometry</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008957" MajorTopicYN="N">Models, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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Butland</name><name sortKey="Gold, B" sort="Gold, B" uniqKey="Gold B" first="B" last="Gold">B. Gold</name><name sortKey="Liu, N L" sort="Liu, N L" uniqKey="Liu N" first="N L" last="Liu">N L Liu</name><name sortKey="Prathapam, R" sort="Prathapam, R" uniqKey="Prathapam R" first="R" last="Prathapam">R. Prathapam</name><name sortKey="Sterling, H J" sort="Sterling, H J" uniqKey="Sterling H" first="H J" last="Sterling">H J Sterling</name><name sortKey="Willams, E R" sort="Willams, E R" uniqKey="Willams E" first="E R" last="Willams">E R Willams</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Yeung, N" sort="Yeung, N" uniqKey="Yeung N" first="N" last="Yeung">N. Yeung</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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