Serveur d'exploration sur la glutarédoxine

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Multi-domain CGFS-type glutaredoxin Grx4 regulates iron homeostasis via direct interaction with a repressor Fep1 in fission yeast.

Identifieur interne : 000933 ( Main/Exploration ); précédent : 000932; suivant : 000934

Multi-domain CGFS-type glutaredoxin Grx4 regulates iron homeostasis via direct interaction with a repressor Fep1 in fission yeast.

Auteurs : Kyoung-Dong Kim [Corée du Sud] ; Hyo-Jin Kim ; Kyung-Chang Lee ; Jung-Hye Roe

Source :

RBID : pubmed:21531205

Descripteurs français

English descriptors

Abstract

The fission yeast Schizosaccharomyces pombe contains two CGFS-type monothiol glutaredoxins, Grx4 and Grx5, which are localized primarily in the nucleus and mitochondria, respectively. We observed involvement of Grx4 in regulating iron-responsive gene expression, which is modulated by a repressor Fep1. Lack of Grx4 caused defects not only in growth but also in the expression of both iron-uptake and iron-utilizing genes regardless of iron availability. In order to unravel how Grx4 is involved in Fep1-mediated regulation, interaction between them was investigated. Co-immunoprecipitation and bimolecular fluorescence complementation (BiFC) revealed that Grx4 physically interacts with Fep1 in vivo. BiFC revealed localized nuclear dots produced by interaction of Grx4 with Fep1. Mutation of cysteine-172 in the CGFS motif to serine (C172S) produced effects similarly observed under Grx4 depletion, such as the loss of iron-dependent gene regulation and the absence of nuclear dots in BiFC analysis. These results suggest that the ability of Grx4 to bind iron, most likely Fe-S cofactor, could be critical in interacting with and modulating the activity of Fep1.

DOI: 10.1016/j.bbrc.2011.04.069
PubMed: 21531205


Affiliations:


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<name sortKey="Kim, Hyo Jin" sort="Kim, Hyo Jin" uniqKey="Kim H" first="Hyo-Jin" last="Kim">Hyo-Jin Kim</name>
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<name sortKey="Lee, Kyung Chang" sort="Lee, Kyung Chang" uniqKey="Lee K" first="Kyung-Chang" last="Lee">Kyung-Chang Lee</name>
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<term>Amino Acid Motifs (MeSH)</term>
<term>GATA Transcription Factors (genetics)</term>
<term>GATA Transcription Factors (metabolism)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Homeostasis (MeSH)</term>
<term>Iron (metabolism)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Schizosaccharomyces (genetics)</term>
<term>Schizosaccharomyces (metabolism)</term>
<term>Schizosaccharomyces pombe Proteins (genetics)</term>
<term>Schizosaccharomyces pombe Proteins (metabolism)</term>
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<term>Facteurs de transcription GATA (génétique)</term>
<term>Facteurs de transcription GATA (métabolisme)</term>
<term>Fer (métabolisme)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
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<term>Motifs d'acides aminés (MeSH)</term>
<term>Protéines de Schizosaccharomyces pombe (génétique)</term>
<term>Protéines de Schizosaccharomyces pombe (métabolisme)</term>
<term>Schizosaccharomyces (génétique)</term>
<term>Schizosaccharomyces (métabolisme)</term>
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<term>Glutaredoxins</term>
<term>Schizosaccharomyces pombe Proteins</term>
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<term>Glutaredoxins</term>
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<term>Motifs d'acides aminés</term>
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<div type="abstract" xml:lang="en">The fission yeast Schizosaccharomyces pombe contains two CGFS-type monothiol glutaredoxins, Grx4 and Grx5, which are localized primarily in the nucleus and mitochondria, respectively. We observed involvement of Grx4 in regulating iron-responsive gene expression, which is modulated by a repressor Fep1. Lack of Grx4 caused defects not only in growth but also in the expression of both iron-uptake and iron-utilizing genes regardless of iron availability. In order to unravel how Grx4 is involved in Fep1-mediated regulation, interaction between them was investigated. Co-immunoprecipitation and bimolecular fluorescence complementation (BiFC) revealed that Grx4 physically interacts with Fep1 in vivo. BiFC revealed localized nuclear dots produced by interaction of Grx4 with Fep1. Mutation of cysteine-172 in the CGFS motif to serine (C172S) produced effects similarly observed under Grx4 depletion, such as the loss of iron-dependent gene regulation and the absence of nuclear dots in BiFC analysis. These results suggest that the ability of Grx4 to bind iron, most likely Fe-S cofactor, could be critical in interacting with and modulating the activity of Fep1.</div>
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