GlutaredoxinV1, Main, Exploration, bibRecord, 000113

The conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2.

Identifieur interne : 000113 ( Main/Exploration ); précédent : 000112; suivant : 000114

The conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2.

Auteurs : Haoran Li [États-Unis] ; Caryn E. Outten [États-Unis]

Source :

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [ 1432-1327 ] ; 2019.

RBID : pubmed:31493153

Descripteurs français

English descriptors

KwdEn :
- Chromatography, Gel (MeSH), Circular Dichroism (MeSH), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Mitochondrial Proteins (chemistry), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Plasmids (genetics), Protein Binding (MeSH), Protein Multimerization (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Trans-Activators (chemistry), Trans-Activators (metabolism).
MESH :
- chemical , chemistry : Iron-Sulfur Proteins, Mitochondrial Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins, Trans-Activators.
- chemical , genetics : Iron-Sulfur Proteins, Mitochondrial Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Iron-Sulfur Proteins, Mitochondrial Proteins, Oxidoreductases, Saccharomyces cerevisiae Proteins, Trans-Activators.
- genetics : Plasmids.
- metabolism : Saccharomyces cerevisiae.
- Chromatography, Gel, Circular Dichroism, Protein Binding, Protein Multimerization.

Abstract

The Saccharomyces cerevisiae transcriptional activator Aft1 and its paralog Aft2 respond to iron deficiency by upregulating expression of proteins required for iron uptake at the plasma membrane, vacuolar iron transport, and mitochondrial iron metabolism, with the net result of mobilizing iron from extracellular sources and intracellular stores. Conversely, when iron levels are sufficient, Aft1 and Aft2 interact with the cytosolic glutaredoxins Grx3 and Grx4 and the BolA protein Bol2, which promote Aft1/2 dissociation from DNA and subsequent export from the nucleus. Previous studies unveiled the molecular mechanism for iron-dependent inhibition of Aft1/2 activity, demonstrating that the [2Fe-2S]-bridged Grx3-Bol2 heterodimer transfers a cluster to Aft2, driving Aft2 dimerization and dissociation from DNA. Here, we provide further insight into the regulation mechanism by investigating the roles of conserved cysteines in Aft2 in iron-sulfur cluster binding and interaction with [2Fe-2S]-Grx3-Bol2. Using size exclusion chromatography and circular dichroism spectroscopy, these studies reveal that both cysteines in the conserved Aft2 Cys-Asp-Cys motif are essential for Aft2 dimerization via [2Fe-2S] cluster binding, while only one cysteine is required for interaction with the [2Fe-2S]-Grx3-Bol2 complex. Taken together, these results provide novel insight into the molecular details of iron-sulfur cluster transfer from Grx3-Bol2 to Aft2 which likely occurs through a ligand exchange mechanism. Loss of either cysteine in the Aft2 iron-sulfur binding site may disrupt this ligand-exchange process leading to the isolation of a trapped Aft2-Grx3-Bol2 intermediate, while the replacement of both cysteines abrogates both the iron-sulfur cluster exchange and the protein-protein interactions between Aft2 and Grx3-Bol2.

DOI: 10.1007/s00775-019-01705-x
PubMed: 31493153
PubMed Central: PMC6800183

Affiliations:

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

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Le document en format XML

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<term>Circular Dichroism (MeSH)</term>
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<term>Iron-Sulfur Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Mitochondrial Proteins (chemistry)</term>
<term>Mitochondrial Proteins (genetics)</term>
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<term>Oxidoreductases (chemistry)</term>
<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Plasmids (genetics)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Multimerization (MeSH)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Trans-Activators (chemistry)</term>
<term>Trans-Activators (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie sur gel (MeSH)</term>
<term>Dichroïsme circulaire (MeSH)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Multimérisation de protéines (MeSH)</term>
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<term>Oxidoreductases (génétique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Plasmides (génétique)</term>
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<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
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<term>Saccharomyces cerevisiae Proteins</term>
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<term>Oxidoreductases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines mitochondriales</term>
<term>Transactivateurs</term>
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<front><div type="abstract" xml:lang="en">The Saccharomyces cerevisiae transcriptional activator Aft1 and its paralog Aft2 respond to iron deficiency by upregulating expression of proteins required for iron uptake at the plasma membrane, vacuolar iron transport, and mitochondrial iron metabolism, with the net result of mobilizing iron from extracellular sources and intracellular stores. Conversely, when iron levels are sufficient, Aft1 and Aft2 interact with the cytosolic glutaredoxins Grx3 and Grx4 and the BolA protein Bol2, which promote Aft1/2 dissociation from DNA and subsequent export from the nucleus. Previous studies unveiled the molecular mechanism for iron-dependent inhibition of Aft1/2 activity, demonstrating that the [2Fe-2S]-bridged Grx3-Bol2 heterodimer transfers a cluster to Aft2, driving Aft2 dimerization and dissociation from DNA. Here, we provide further insight into the regulation mechanism by investigating the roles of conserved cysteines in Aft2 in iron-sulfur cluster binding and interaction with [2Fe-2S]-Grx3-Bol2. Using size exclusion chromatography and circular dichroism spectroscopy, these studies reveal that both cysteines in the conserved Aft2 Cys-Asp-Cys motif are essential for Aft2 dimerization via [2Fe-2S] cluster binding, while only one cysteine is required for interaction with the [2Fe-2S]-Grx3-Bol2 complex. Taken together, these results provide novel insight into the molecular details of iron-sulfur cluster transfer from Grx3-Bol2 to Aft2 which likely occurs through a ligand exchange mechanism. Loss of either cysteine in the Aft2 iron-sulfur binding site may disrupt this ligand-exchange process leading to the isolation of a trapped Aft2-Grx3-Bol2 intermediate, while the replacement of both cysteines abrogates both the iron-sulfur cluster exchange and the protein-protein interactions between Aft2 and Grx3-Bol2.</div>
</front>
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<Abstract><AbstractText>The Saccharomyces cerevisiae transcriptional activator Aft1 and its paralog Aft2 respond to iron deficiency by upregulating expression of proteins required for iron uptake at the plasma membrane, vacuolar iron transport, and mitochondrial iron metabolism, with the net result of mobilizing iron from extracellular sources and intracellular stores. Conversely, when iron levels are sufficient, Aft1 and Aft2 interact with the cytosolic glutaredoxins Grx3 and Grx4 and the BolA protein Bol2, which promote Aft1/2 dissociation from DNA and subsequent export from the nucleus. Previous studies unveiled the molecular mechanism for iron-dependent inhibition of Aft1/2 activity, demonstrating that the [2Fe-2S]-bridged Grx3-Bol2 heterodimer transfers a cluster to Aft2, driving Aft2 dimerization and dissociation from DNA. Here, we provide further insight into the regulation mechanism by investigating the roles of conserved cysteines in Aft2 in iron-sulfur cluster binding and interaction with [2Fe-2S]-Grx3-Bol2. Using size exclusion chromatography and circular dichroism spectroscopy, these studies reveal that both cysteines in the conserved Aft2 Cys-Asp-Cys motif are essential for Aft2 dimerization via [2Fe-2S] cluster binding, while only one cysteine is required for interaction with the [2Fe-2S]-Grx3-Bol2 complex. Taken together, these results provide novel insight into the molecular details of iron-sulfur cluster transfer from Grx3-Bol2 to Aft2 which likely occurs through a ligand exchange mechanism. Loss of either cysteine in the Aft2 iron-sulfur binding site may disrupt this ligand-exchange process leading to the isolation of a trapped Aft2-Grx3-Bol2 intermediate, while the replacement of both cysteines abrogates both the iron-sulfur cluster exchange and the protein-protein interactions between Aft2 and Grx3-Bol2.</AbstractText>
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<Keyword MajorTopicYN="Y">Iron regulation</Keyword>
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<ReferenceList><Reference><Citation>J Biol Chem. 2001 Sep 7;276(36):34221-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11448968</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14322-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11734641</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2002 May 24;277(21):18914-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11877447</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 Jul 25;278(30):27636-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12756250</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genetics. 2005 Jan;169(1):107-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15489514</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Mar 18;280(11):10135-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15649888</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2005 Aug;25(15):6760-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16024809</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Jun 30;281(26):17661-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16648636</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Sci. 2006 Nov 1;119(Pt 21):4554-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17074835</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 2007 Aug;18(8):2980-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17538022</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2007 Dec 25;46(51):15018-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18044966</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Apr 18;283(16):10276-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18281282</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2009 Oct 13;48(40):9569-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19715344</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Metab. 2010 Oct 6;12(4):373-385</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20889129</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2011 Jan 7;286(1):867-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20978135</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2012 Jun 5;51(22):4377-89</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22583368</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2012 Dec;32(24):4998-5008</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23045394</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2014 Mar 18;111(11):4043-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24591629</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1995 Mar 15;14(6):1231-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7720713</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1996 Jul 1;15(13):3377-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8670839</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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The conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2.

The conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2.

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