GlutaredoxinV1, Main, Exploration, bibRecord, 000A69

The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.

Identifieur interne : 000A69 ( Main/Exploration ); précédent : 000A68; suivant : 000A70

The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.

Auteurs : Haoran Li [États-Unis] ; Daphne T. Mapolelo ; Nin N. Dingra ; Sunil G. Naik ; Nicholas S. Lees ; Brian M. Hoffman ; Pamela J. Riggs-Gelasco ; Boi Hanh Huynh ; Michael K. Johnson ; Caryn E. Outten

Source :

Biochemistry [ 1520-4995 ] ; 2009.

RBID : pubmed:19715344

Descripteurs français

English descriptors

KwdEn :
- Cysteine (genetics), Cysteine (metabolism), Dimerization (MeSH), Enzyme Stability (genetics), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Fungal (MeSH), Glutaredoxins (biosynthesis), Glutaredoxins (chemistry), Glutaredoxins (genetics), Histidine (genetics), Histidine (metabolism), Intracellular Signaling Peptides and Proteins (chemistry), Intracellular Signaling Peptides and Proteins (genetics), Iron-Sulfur Proteins (biosynthesis), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Ligands (MeSH), Multiprotein Complexes (biosynthesis), Multiprotein Complexes (chemistry), Multiprotein Complexes (genetics), Mutagenesis, Site-Directed (MeSH), Oxidoreductases (biosynthesis), Oxidoreductases (chemistry), Oxidoreductases (genetics), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (biosynthesis), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Signal Transduction (genetics).
MESH :
- chemical , biosynthesis : Glutaredoxins, Iron-Sulfur Proteins, Multiprotein Complexes, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , chemistry : Glutaredoxins, Intracellular Signaling Peptides and Proteins, Iron-Sulfur Proteins, Multiprotein Complexes, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Cysteine, Glutaredoxins, Histidine, Intracellular Signaling Peptides and Proteins, Iron-Sulfur Proteins, Multiprotein Complexes, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Cysteine, Histidine.
- chemistry : Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Enzyme Stability, Saccharomyces cerevisiae, Signal Transduction.
- Dimerization, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Ligands, Mutagenesis, Site-Directed.

Abstract

The transcription of iron uptake and storage genes in Saccharomyces cerevisiae is primarily regulated by the transcription factor Aft1. Nucleocytoplasmic shuttling of Aft1 is dependent upon mitochondrial Fe-S cluster biosynthesis via a signaling pathway that includes the cytosolic monothiol glutaredoxins (Grx3 and Grx4) and the BolA homologue Fra2. However, the interactions between these proteins and the iron-dependent mechanism by which they control Aft1 localization are unclear. To reconstitute and characterize components of this signaling pathway in vitro, we have overexpressed yeast Fra2 and Grx3/4 in Escherichia coli. We have shown that coexpression of recombinant Fra2 with Grx3 or Grx4 allows purification of a stable [2Fe-2S](2+) cluster-containing Fra2-Grx3 or Fra2-Grx4 heterodimeric complex. Reconstitution of a [2Fe-2S] cluster on Grx3 or Grx4 without Fra2 produces a [2Fe-2S]-bridged homodimer. UV-visible absorption and CD, resonance Raman, EPR, ENDOR, Mossbauer, and EXAFS studies of [2Fe-2S] Grx3/4 homodimers and the [2Fe-2S] Fra2-Grx3/4 heterodimers indicate that inclusion of Fra2 in the Grx3/4 Fe-S complex causes a change in the cluster stability and coordination environment. Taken together, our analytical, spectroscopic, and mutagenesis data indicate that Grx3/4 and Fra2 form a Fe-S-bridged heterodimeric complex with Fe ligands provided by the active site cysteine of Grx3/4, glutathione, and a histidine residue. Overall, these results suggest that the ability of the Fra2-Grx3/4 complex to assemble a [2Fe-2S] cluster may act as a signal to control the iron regulon in response to cellular iron status in yeast.

DOI: 10.1021/bi901182w
PubMed: 19715344
PubMed Central: PMC2796373

Affiliations:

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<term>Cysteine (metabolism)</term>
<term>Dimerization (MeSH)</term>
<term>Enzyme Stability (genetics)</term>
<term>Gene Expression Regulation, Enzymologic (MeSH)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Glutaredoxins (biosynthesis)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Histidine (genetics)</term>
<term>Histidine (metabolism)</term>
<term>Intracellular Signaling Peptides and Proteins (chemistry)</term>
<term>Intracellular Signaling Peptides and Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (biosynthesis)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
<term>Ligands (MeSH)</term>
<term>Multiprotein Complexes (biosynthesis)</term>
<term>Multiprotein Complexes (chemistry)</term>
<term>Multiprotein Complexes (genetics)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Oxidoreductases (biosynthesis)</term>
<term>Oxidoreductases (chemistry)</term>
<term>Oxidoreductases (genetics)</term>
<term>Saccharomyces cerevisiae (chemistry)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (biosynthesis)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Signal Transduction (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Complexes multiprotéiques (biosynthèse)</term>
<term>Complexes multiprotéiques (composition chimique)</term>
<term>Complexes multiprotéiques (génétique)</term>
<term>Cystéine (génétique)</term>
<term>Cystéine (métabolisme)</term>
<term>Dimérisation (MeSH)</term>
<term>Ferrosulfoprotéines (biosynthèse)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Glutarédoxines (biosynthèse)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Histidine (génétique)</term>
<term>Histidine (métabolisme)</term>
<term>Ligands (MeSH)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Oxidoreductases (biosynthèse)</term>
<term>Oxidoreductases (composition chimique)</term>
<term>Oxidoreductases (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (biosynthèse)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines et peptides de signalisation intracellulaire (composition chimique)</term>
<term>Protéines et peptides de signalisation intracellulaire (génétique)</term>
<term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharomyces cerevisiae (composition chimique)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Stabilité enzymatique (génétique)</term>
<term>Transduction du signal (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
<term>Multiprotein Complexes</term>
<term>Oxidoreductases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term>
<term>Intracellular Signaling Peptides and Proteins</term>
<term>Iron-Sulfur Proteins</term>
<term>Multiprotein Complexes</term>
<term>Oxidoreductases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine</term>
<term>Glutaredoxins</term>
<term>Histidine</term>
<term>Intracellular Signaling Peptides and Proteins</term>
<term>Iron-Sulfur Proteins</term>
<term>Multiprotein Complexes</term>
<term>Oxidoreductases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term>
<term>Histidine</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Oxidoreductases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Oxidoreductases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines et peptides de signalisation intracellulaire</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Enzyme Stability</term>
<term>Saccharomyces cerevisiae</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Cystéine</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Histidine</term>
<term>Oxidoreductases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines et peptides de signalisation intracellulaire</term>
<term>Saccharomyces cerevisiae</term>
<term>Stabilité enzymatique</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cystéine</term>
<term>Histidine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Dimerization</term>
<term>Gene Expression Regulation, Enzymologic</term>
<term>Gene Expression Regulation, Fungal</term>
<term>Ligands</term>
<term>Mutagenesis, Site-Directed</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Dimérisation</term>
<term>Ligands</term>
<term>Mutagenèse dirigée</term>
<term>Régulation de l'expression des gènes codant pour des enzymes</term>
<term>Régulation de l'expression des gènes fongiques</term>
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<front><div type="abstract" xml:lang="en">The transcription of iron uptake and storage genes in Saccharomyces cerevisiae is primarily regulated by the transcription factor Aft1. Nucleocytoplasmic shuttling of Aft1 is dependent upon mitochondrial Fe-S cluster biosynthesis via a signaling pathway that includes the cytosolic monothiol glutaredoxins (Grx3 and Grx4) and the BolA homologue Fra2. However, the interactions between these proteins and the iron-dependent mechanism by which they control Aft1 localization are unclear. To reconstitute and characterize components of this signaling pathway in vitro, we have overexpressed yeast Fra2 and Grx3/4 in Escherichia coli. We have shown that coexpression of recombinant Fra2 with Grx3 or Grx4 allows purification of a stable [2Fe-2S](2+) cluster-containing Fra2-Grx3 or Fra2-Grx4 heterodimeric complex. Reconstitution of a [2Fe-2S] cluster on Grx3 or Grx4 without Fra2 produces a [2Fe-2S]-bridged homodimer. UV-visible absorption and CD, resonance Raman, EPR, ENDOR, Mossbauer, and EXAFS studies of [2Fe-2S] Grx3/4 homodimers and the [2Fe-2S] Fra2-Grx3/4 heterodimers indicate that inclusion of Fra2 in the Grx3/4 Fe-S complex causes a change in the cluster stability and coordination environment. Taken together, our analytical, spectroscopic, and mutagenesis data indicate that Grx3/4 and Fra2 form a Fe-S-bridged heterodimeric complex with Fe ligands provided by the active site cysteine of Grx3/4, glutathione, and a histidine residue. Overall, these results suggest that the ability of the Fra2-Grx3/4 complex to assemble a [2Fe-2S] cluster may act as a signal to control the iron regulon in response to cellular iron status in yeast.</div>
</front>
</TEI>
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<DateCompleted><Year>2009</Year>
<Month>12</Month>
<Day>03</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>48</Volume>
<Issue>40</Issue>
<PubDate><Year>2009</Year>
<Month>Oct</Month>
<Day>13</Day>
</PubDate>
</JournalIssue>
<Title>Biochemistry</Title>
<ISOAbbreviation>Biochemistry</ISOAbbreviation>
</Journal>
<ArticleTitle>The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.</ArticleTitle>
<Pagination><MedlinePgn>9569-81</MedlinePgn>
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<ELocationID EIdType="doi" ValidYN="Y">10.1021/bi901182w</ELocationID>
<Abstract><AbstractText>The transcription of iron uptake and storage genes in Saccharomyces cerevisiae is primarily regulated by the transcription factor Aft1. Nucleocytoplasmic shuttling of Aft1 is dependent upon mitochondrial Fe-S cluster biosynthesis via a signaling pathway that includes the cytosolic monothiol glutaredoxins (Grx3 and Grx4) and the BolA homologue Fra2. However, the interactions between these proteins and the iron-dependent mechanism by which they control Aft1 localization are unclear. To reconstitute and characterize components of this signaling pathway in vitro, we have overexpressed yeast Fra2 and Grx3/4 in Escherichia coli. We have shown that coexpression of recombinant Fra2 with Grx3 or Grx4 allows purification of a stable [2Fe-2S](2+) cluster-containing Fra2-Grx3 or Fra2-Grx4 heterodimeric complex. Reconstitution of a [2Fe-2S] cluster on Grx3 or Grx4 without Fra2 produces a [2Fe-2S]-bridged homodimer. UV-visible absorption and CD, resonance Raman, EPR, ENDOR, Mossbauer, and EXAFS studies of [2Fe-2S] Grx3/4 homodimers and the [2Fe-2S] Fra2-Grx3/4 heterodimers indicate that inclusion of Fra2 in the Grx3/4 Fe-S complex causes a change in the cluster stability and coordination environment. Taken together, our analytical, spectroscopic, and mutagenesis data indicate that Grx3/4 and Fra2 form a Fe-S-bridged heterodimeric complex with Fe ligands provided by the active site cysteine of Grx3/4, glutathione, and a histidine residue. Overall, these results suggest that the ability of the Fra2-Grx3/4 complex to assemble a [2Fe-2S] cluster may act as a signal to control the iron regulon in response to cellular iron status in yeast.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Haoran</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Mapolelo</LastName>
<ForeName>Daphne T</ForeName>
<Initials>DT</Initials>
</Author>
<Author ValidYN="Y"><LastName>Dingra</LastName>
<ForeName>Nin N</ForeName>
<Initials>NN</Initials>
</Author>
<Author ValidYN="Y"><LastName>Naik</LastName>
<ForeName>Sunil G</ForeName>
<Initials>SG</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lees</LastName>
<ForeName>Nicholas S</ForeName>
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</Author>
<Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Michael K</ForeName>
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<Author ValidYN="Y"><LastName>Outten</LastName>
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The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.

The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.

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