GlutaredoxinV1, Main, Exploration, bibRecord, 000B47

Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1.

Identifieur interne : 000B47 ( Main/Exploration ); précédent : 000B46; suivant : 000B48

Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1.

Auteurs : Alexandre Mercier [Canada] ; Simon Labbé

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2009.

RBID : pubmed:19502236

Descripteurs français

English descriptors

KwdEn :
- CCAAT-Binding Factor (analysis), CCAAT-Binding Factor (genetics), CCAAT-Binding Factor (metabolism), Cell Nucleus (metabolism), Cytoplasm (metabolism), GATA Transcription Factors (metabolism), Gene Expression Regulation (MeSH), Glutaredoxins (metabolism), Iron (metabolism), Karyopherins (metabolism), Protein Transport (MeSH), Receptors, Cytoplasmic and Nuclear (metabolism), Schizosaccharomyces (cytology), Schizosaccharomyces (metabolism), Schizosaccharomyces pombe Proteins (analysis), Schizosaccharomyces pombe Proteins (genetics), Schizosaccharomyces pombe Proteins (metabolism).
MESH :
- chemical , analysis : CCAAT-Binding Factor, Schizosaccharomyces pombe Proteins.
- chemical , genetics : CCAAT-Binding Factor, Schizosaccharomyces pombe Proteins.
- chemical , metabolism : CCAAT-Binding Factor, GATA Transcription Factors, Glutaredoxins, Iron, Karyopherins, Receptors, Cytoplasmic and Nuclear, Schizosaccharomyces pombe Proteins.
- cytology : Schizosaccharomyces.
- metabolism : Cell Nucleus, Cytoplasm, Schizosaccharomyces.
- Gene Expression Regulation, Protein Transport.

Abstract

In Schizosaccharomyces pombe, the CCAAT-binding factor is a multisubunit complex that contains the proteins Php2, Php3, Php4, and Php5. Under low iron conditions, Php4 acts as a negative regulatory subunit of the CCAAT-binding factor and fosters repression of genes encoding iron-using proteins. Under conditions of iron excess, Php4 expression is turned off by the iron-dependent transcriptional repressor Fep1. In this study, we developed a biological system that allows us to unlink iron-dependent behavior of Php4 protein from its transcriptional regulation by Fep1. Microscopic analyses revealed that a functional GFP-Php4 protein accumulates in the nucleus under conditions of iron starvation. Conversely, in cells undergoing a transition from low to high iron, GFP-Php4 is exported from the nucleus to the cytoplasm. We mapped a leucine-rich nuclear export signal that is necessary for nuclear exclusion of Php4. This latter process was blocked by leptomycin B. By using coimmunoprecipitation analysis, we showed that Php4 and Crm1 physically interact with each other. Although we determined that nuclear retention of Php4 per se is not sufficient to cause a constitutive repression of iron-using genes, we found that deletion of the grx4(+)-encoded glutaredoxin-4 renders Php4 constitutively active and invariably localized in the nucleus. Further analysis by bimolecular fluorescence complementation assay and by two-hybrid assays showed that Php4 and Grx4 are physically associated in vivo. Taken together, our findings indicate that Grx4 and Crm1 are novel components involved in the mechanism by which Php4 is inactivated by iron in a Fep1-independent manner.

DOI: 10.1074/jbc.M109.009563
PubMed: 19502236
PubMed Central: PMC2740451

Affiliations:

Canada

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

to stream Main, to step Corpus: 000B00
to stream Main, to step Curation: 000B00

Le document en format XML

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<term>Facteur de liaison à la séquence CCAAT (génétique)</term>
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<term>Protéines de Schizosaccharomyces pombe (génétique)</term>
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<term>Régulation de l'expression des gènes (MeSH)</term>
<term>Schizosaccharomyces (cytologie)</term>
<term>Schizosaccharomyces (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">In Schizosaccharomyces pombe, the CCAAT-binding factor is a multisubunit complex that contains the proteins Php2, Php3, Php4, and Php5. Under low iron conditions, Php4 acts as a negative regulatory subunit of the CCAAT-binding factor and fosters repression of genes encoding iron-using proteins. Under conditions of iron excess, Php4 expression is turned off by the iron-dependent transcriptional repressor Fep1. In this study, we developed a biological system that allows us to unlink iron-dependent behavior of Php4 protein from its transcriptional regulation by Fep1. Microscopic analyses revealed that a functional GFP-Php4 protein accumulates in the nucleus under conditions of iron starvation. Conversely, in cells undergoing a transition from low to high iron, GFP-Php4 is exported from the nucleus to the cytoplasm. We mapped a leucine-rich nuclear export signal that is necessary for nuclear exclusion of Php4. This latter process was blocked by leptomycin B. By using coimmunoprecipitation analysis, we showed that Php4 and Crm1 physically interact with each other. Although we determined that nuclear retention of Php4 per se is not sufficient to cause a constitutive repression of iron-using genes, we found that deletion of the grx4(+)-encoded glutaredoxin-4 renders Php4 constitutively active and invariably localized in the nucleus. Further analysis by bimolecular fluorescence complementation assay and by two-hybrid assays showed that Php4 and Grx4 are physically associated in vivo. Taken together, our findings indicate that Grx4 and Crm1 are novel components involved in the mechanism by which Php4 is inactivated by iron in a Fep1-independent manner.</div>
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<Abstract><AbstractText>In Schizosaccharomyces pombe, the CCAAT-binding factor is a multisubunit complex that contains the proteins Php2, Php3, Php4, and Php5. Under low iron conditions, Php4 acts as a negative regulatory subunit of the CCAAT-binding factor and fosters repression of genes encoding iron-using proteins. Under conditions of iron excess, Php4 expression is turned off by the iron-dependent transcriptional repressor Fep1. In this study, we developed a biological system that allows us to unlink iron-dependent behavior of Php4 protein from its transcriptional regulation by Fep1. Microscopic analyses revealed that a functional GFP-Php4 protein accumulates in the nucleus under conditions of iron starvation. Conversely, in cells undergoing a transition from low to high iron, GFP-Php4 is exported from the nucleus to the cytoplasm. We mapped a leucine-rich nuclear export signal that is necessary for nuclear exclusion of Php4. This latter process was blocked by leptomycin B. By using coimmunoprecipitation analysis, we showed that Php4 and Crm1 physically interact with each other. Although we determined that nuclear retention of Php4 per se is not sufficient to cause a constitutive repression of iron-using genes, we found that deletion of the grx4(+)-encoded glutaredoxin-4 renders Php4 constitutively active and invariably localized in the nucleus. Further analysis by bimolecular fluorescence complementation assay and by two-hybrid assays showed that Php4 and Grx4 are physically associated in vivo. Taken together, our findings indicate that Grx4 and Crm1 are novel components involved in the mechanism by which Php4 is inactivated by iron in a Fep1-independent manner.</AbstractText>
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Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1.

Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1.

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