GlutaredoxinV1, Main, Exploration, bibRecord, 000313

Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.

Identifieur interne : 000313 ( Main/Exploration ); précédent : 000312; suivant : 000314

Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.

Auteurs : Adrienne C. Dlouhy [États-Unis] ; Jude Beaudoin ; Simon Labbé ; Caryn E. Outten

Source :

Metallomics : integrated biometal science [ 1756-591X ] ; 2017.

RBID : pubmed:28725905

Descripteurs français

English descriptors

KwdEn :
- CCAAT-Binding Factor (genetics), CCAAT-Binding Factor (metabolism), Cysteine (metabolism), Gene Expression Regulation, Fungal (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Iron (metabolism), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Models, Molecular (MeSH), Schizosaccharomyces (growth & development), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism), Signal Transduction (MeSH).
MESH :
- chemical , genetics : CCAAT-Binding Factor, Glutaredoxins, Iron-Sulfur Proteins, Schizosaccharomyces pombe Proteins.
- chemical , metabolism : CCAAT-Binding Factor, Cysteine, Glutaredoxins, Iron, Iron-Sulfur Proteins, Schizosaccharomyces pombe Proteins.
- growth & development : Schizosaccharomyces.
- metabolism : Schizosaccharomyces.
- Gene Expression Regulation, Fungal, Models, Molecular, Signal Transduction.

Abstract

The fission yeast Schizosaccharomyces pombe expresses the CCAAT-binding factor Php4 in response to iron deprivation. Php4 forms a transcription complex with Php2, Php3, and Php5 to repress the expression of iron proteins as a means to economize iron usage. Previous in vivo results demonstrate that the function and location of Php4 are regulated in an iron-dependent manner by the cytosolic CGFS type glutaredoxin Grx4. In this study, we aimed to biochemically define these protein-protein and protein-metal interactions. Grx4 was found to bind a [2Fe-2S] cluster with spectroscopic features similar to other CGFS glutaredoxins. Grx4 and Php4 also copurify as a complex with a [2Fe-2S] cluster that is spectroscopically distinct from the cluster on Grx4 alone. In vitro titration experiments suggest that these Fe-S complexes may not be interconvertible in the absence of additional factors. Furthermore, conserved cysteines in Grx4 (Cys172) and Php4 (Cys221 and Cys227) are necessary for Fe-S cluster binding and stable complex formation. Together, these results show that Grx4 controls Php4 function through binding of a bridging [2Fe-2S] cluster.

DOI: 10.1039/c7mt00144d
PubMed: 28725905
PubMed Central: PMC5595146

Affiliations:

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

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Le document en format XML

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<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Iron (metabolism)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
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<term>Schizosaccharomyces (metabolism)</term>
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<term>Schizosaccharomyces pombe Proteins (metabolism)</term>
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<term>Facteur de liaison à la séquence CCAAT (génétique)</term>
<term>Facteur de liaison à la séquence CCAAT (métabolisme)</term>
<term>Fer (métabolisme)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Protéines de Schizosaccharomyces pombe (génétique)</term>
<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Schizosaccharomyces (croissance et développement)</term>
<term>Schizosaccharomyces (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
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<term>Glutaredoxins</term>
<term>Iron-Sulfur Proteins</term>
<term>Schizosaccharomyces pombe Proteins</term>
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<term>Cysteine</term>
<term>Glutaredoxins</term>
<term>Iron</term>
<term>Iron-Sulfur Proteins</term>
<term>Schizosaccharomyces pombe Proteins</term>
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<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Protéines de Schizosaccharomyces pombe</term>
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<term>Facteur de liaison à la séquence CCAAT</term>
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<front><div type="abstract" xml:lang="en">The fission yeast Schizosaccharomyces pombe expresses the CCAAT-binding factor Php4 in response to iron deprivation. Php4 forms a transcription complex with Php2, Php3, and Php5 to repress the expression of iron proteins as a means to economize iron usage. Previous in vivo results demonstrate that the function and location of Php4 are regulated in an iron-dependent manner by the cytosolic CGFS type glutaredoxin Grx4. In this study, we aimed to biochemically define these protein-protein and protein-metal interactions. Grx4 was found to bind a [2Fe-2S] cluster with spectroscopic features similar to other CGFS glutaredoxins. Grx4 and Php4 also copurify as a complex with a [2Fe-2S] cluster that is spectroscopically distinct from the cluster on Grx4 alone. In vitro titration experiments suggest that these Fe-S complexes may not be interconvertible in the absence of additional factors. Furthermore, conserved cysteines in Grx4 (Cys172) and Php4 (Cys221 and Cys227) are necessary for Fe-S cluster binding and stable complex formation. Together, these results show that Grx4 controls Php4 function through binding of a bridging [2Fe-2S] cluster.</div>
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<Abstract><AbstractText>The fission yeast Schizosaccharomyces pombe expresses the CCAAT-binding factor Php4 in response to iron deprivation. Php4 forms a transcription complex with Php2, Php3, and Php5 to repress the expression of iron proteins as a means to economize iron usage. Previous in vivo results demonstrate that the function and location of Php4 are regulated in an iron-dependent manner by the cytosolic CGFS type glutaredoxin Grx4. In this study, we aimed to biochemically define these protein-protein and protein-metal interactions. Grx4 was found to bind a [2Fe-2S] cluster with spectroscopic features similar to other CGFS glutaredoxins. Grx4 and Php4 also copurify as a complex with a [2Fe-2S] cluster that is spectroscopically distinct from the cluster on Grx4 alone. In vitro titration experiments suggest that these Fe-S complexes may not be interconvertible in the absence of additional factors. Furthermore, conserved cysteines in Grx4 (Cys172) and Php4 (Cys221 and Cys227) are necessary for Fe-S cluster binding and stable complex formation. Together, these results show that Grx4 controls Php4 function through binding of a bridging [2Fe-2S] cluster.</AbstractText>
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   |texte=   Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.
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Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.

Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.

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