DetoxFungiV1, Main, Exploration, bibRecord, 001C77

Cnh1 Na(+) /H(+) antiporter and Ena1 Na(+) -ATPase play different roles in cation homeostasis and cell physiology of Candida glabrata.

Identifieur interne : 001C77 ( Main/Exploration ); précédent : 001C76; suivant : 001C78

Cnh1 Na(+) /H(+) antiporter and Ena1 Na(+) -ATPase play different roles in cation homeostasis and cell physiology of Candida glabrata.

Auteurs : Yannick Krauke [République tchèque] ; Hana Sychrova

Source :

FEMS yeast research [ 1567-1364 ] ; 2011.

RBID : pubmed:20942808

Descripteurs français

English descriptors

KwdEn :
- Candida glabrata (genetics), Candida glabrata (metabolism), Candida glabrata (physiology), Cations (metabolism), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Deletion (MeSH), Gene Expression Regulation, Fungal (MeSH), Genetic Complementation Test (MeSH), Homeostasis (MeSH), Potassium (metabolism), Saccharomyces cerevisiae (metabolism), Sodium (metabolism), Sodium-Hydrogen Exchangers (genetics), Sodium-Hydrogen Exchangers (metabolism), Substrate Specificity (MeSH).
MESH :
- chemical , genetics : Fungal Proteins, Sodium-Hydrogen Exchangers.
- chemical , metabolism : Cations, Fungal Proteins, Potassium, Sodium, Sodium-Hydrogen Exchangers.
- genetics : Candida glabrata.
- metabolism : Candida glabrata, Saccharomyces cerevisiae.
- physiology : Candida glabrata.
- Gene Deletion, Gene Expression Regulation, Fungal, Genetic Complementation Test, Homeostasis, Substrate Specificity.

Abstract

Yeasts tightly regulate their intracellular concentrations of alkali metal cations. In Saccharomyces cerevisiae, the Nha1 Na(+) /H(+) -antiporter and Ena1 Na(+) -ATPase, mediate the efflux of toxic sodium and surplus potassium. We report the characterization of Candida glabrata CgCnh1 and CgEna1 homologues. Their substrate specificity and transport properties were compared upon expression in S. cerevisiae, and their function characterized directly in C. glabrata. The CgCnh1 antiporter and the CgEna1 ATPase transport both potassium and sodium when expressed in S. cerevisiae. CgEna1p fully complements the lack of S. cerevisiae own Na(+) -ATPases but the activity of the CgCnh1 antiporter is lower than that of ScNha1p. Candida glabrata deletion mutants and analyses of their phenotypes revealed that though both transporters have a broad substrate specificity, their function in C. glabrata cells is not the same. Their differing physiological roles are also reflected in their regulation of expression, CgENA1 is highly upregulated by an increased osmotic pressure or sodium concentration, whereas CgCNH1 is expressed constitutively. The Cnh1 antiporter is involved in the regulation of potassium content and the Ena1 ATPase in sodium detoxification of C. glabrata cells. This situation differs from S. cerevisiae, where the Nha1 antiporter and Ena ATPases both participate together in Na(+) detoxification and in the regulation of K(+) homeostasis.

DOI: 10.1111/j.1567-1364.2010.00686.x
PubMed: 20942808

Affiliations:

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Le document en format XML

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<term>Cations (metabolism)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Deletion (MeSH)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Genetic Complementation Test (MeSH)</term>
<term>Homeostasis (MeSH)</term>
<term>Potassium (metabolism)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Sodium (metabolism)</term>
<term>Sodium-Hydrogen Exchangers (genetics)</term>
<term>Sodium-Hydrogen Exchangers (metabolism)</term>
<term>Substrate Specificity (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Antiport des ions sodium-hydrogène (génétique)</term>
<term>Antiport des ions sodium-hydrogène (métabolisme)</term>
<term>Candida glabrata (génétique)</term>
<term>Candida glabrata (métabolisme)</term>
<term>Candida glabrata (physiologie)</term>
<term>Cations (métabolisme)</term>
<term>Délétion de gène (MeSH)</term>
<term>Homéostasie (MeSH)</term>
<term>Potassium (métabolisme)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sodium (métabolisme)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Test de complémentation (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>Sodium-Hydrogen Exchangers</term>
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<term>Potassium</term>
<term>Sodium</term>
<term>Sodium-Hydrogen Exchangers</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Candida glabrata</term>
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<term>Candida glabrata</term>
<term>Protéines fongiques</term>
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<term>Potassium</term>
<term>Protéines fongiques</term>
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<keywords scheme="MESH" xml:lang="en"><term>Gene Deletion</term>
<term>Gene Expression Regulation, Fungal</term>
<term>Genetic Complementation Test</term>
<term>Homeostasis</term>
<term>Substrate Specificity</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Délétion de gène</term>
<term>Homéostasie</term>
<term>Régulation de l'expression des gènes fongiques</term>
<term>Spécificité du substrat</term>
<term>Test de complémentation</term>
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<front><div type="abstract" xml:lang="en">Yeasts tightly regulate their intracellular concentrations of alkali metal cations. In Saccharomyces cerevisiae, the Nha1 Na(+) /H(+) -antiporter and Ena1 Na(+) -ATPase, mediate the efflux of toxic sodium and surplus potassium. We report the characterization of Candida glabrata CgCnh1 and CgEna1 homologues. Their substrate specificity and transport properties were compared upon expression in S. cerevisiae, and their function characterized directly in C. glabrata. The CgCnh1 antiporter and the CgEna1 ATPase transport both potassium and sodium when expressed in S. cerevisiae. CgEna1p fully complements the lack of S. cerevisiae own Na(+) -ATPases but the activity of the CgCnh1 antiporter is lower than that of ScNha1p. Candida glabrata deletion mutants and analyses of their phenotypes revealed that though both transporters have a broad substrate specificity, their function in C. glabrata cells is not the same. Their differing physiological roles are also reflected in their regulation of expression, CgENA1 is highly upregulated by an increased osmotic pressure or sodium concentration, whereas CgCNH1 is expressed constitutively. The Cnh1 antiporter is involved in the regulation of potassium content and the Ena1 ATPase in sodium detoxification of C. glabrata cells. This situation differs from S. cerevisiae, where the Nha1 antiporter and Ena ATPases both participate together in Na(+) detoxification and in the regulation of K(+) homeostasis.</div>
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<Abstract><AbstractText>Yeasts tightly regulate their intracellular concentrations of alkali metal cations. In Saccharomyces cerevisiae, the Nha1 Na(+) /H(+) -antiporter and Ena1 Na(+) -ATPase, mediate the efflux of toxic sodium and surplus potassium. We report the characterization of Candida glabrata CgCnh1 and CgEna1 homologues. Their substrate specificity and transport properties were compared upon expression in S. cerevisiae, and their function characterized directly in C. glabrata. The CgCnh1 antiporter and the CgEna1 ATPase transport both potassium and sodium when expressed in S. cerevisiae. CgEna1p fully complements the lack of S. cerevisiae own Na(+) -ATPases but the activity of the CgCnh1 antiporter is lower than that of ScNha1p. Candida glabrata deletion mutants and analyses of their phenotypes revealed that though both transporters have a broad substrate specificity, their function in C. glabrata cells is not the same. Their differing physiological roles are also reflected in their regulation of expression, CgENA1 is highly upregulated by an increased osmotic pressure or sodium concentration, whereas CgCNH1 is expressed constitutively. The Cnh1 antiporter is involved in the regulation of potassium content and the Ena1 ATPase in sodium detoxification of C. glabrata cells. This situation differs from S. cerevisiae, where the Nha1 antiporter and Ena ATPases both participate together in Na(+) detoxification and in the regulation of K(+) homeostasis.</AbstractText>
<CopyrightInformation>© 2010 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.</CopyrightInformation>
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Cnh1 Na(+) /H(+) antiporter and Ena1 Na(+) -ATPase play different roles in cation homeostasis and cell physiology of Candida glabrata.

Cnh1 Na(+) /H(+) antiporter and Ena1 Na(+) -ATPase play different roles in cation homeostasis and cell physiology of Candida glabrata.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki