Abstract
The isolation and functional characterization of a Candida albicans Na+/H+ antiporter gene, CNH1, is reported here. The gene encodes a protein of 840 amino acids that exhibits high levels of similarity in sequence, size, and structural and functional domains to a group of known Na+/H+ antiporters of fungi. The CNH1 gene is able to functionally complement the salt-sensitivity of a Saccharomyces cerevisiae ena1 nha1 mutant, and mutations of two conserved aspartate residues to asparagines in the putative Na+-binding site abolish this activity. Deletion of CNH1 results in retardation of growth and a highly elongated morphology in a significant fraction of cells under conditions that normally support yeast growth. These results indicate that CNH1 has a role in Na+ and H+ transport, salt-tolerance, and morphogenesis.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / metabolism
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Amino Acid Sequence
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Animals
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Base Sequence
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Candida albicans / genetics*
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Candida albicans / growth & development
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Candida albicans / metabolism
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Cation Transport Proteins*
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Cloning, Molecular
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Galactose
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Gene Deletion
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Genes, Fungal*
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Hydrogen-Ion Concentration
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Membrane Proteins / metabolism
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Mutation
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins*
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Sodium Chloride
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Sodium-Hydrogen Exchanger 1
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Sodium-Hydrogen Exchangers / genetics*
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Sodium-Hydrogen Exchangers / metabolism
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Sodium-Potassium-Exchanging ATPase
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Transformation, Genetic
Substances
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Cation Transport Proteins
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ENA1 protein, S cerevisiae
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Membrane Proteins
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NHA1 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Slc9a1 protein, mouse
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Sodium-Hydrogen Exchanger 1
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Sodium-Hydrogen Exchangers
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Sodium Chloride
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Adenosine Triphosphatases
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Sodium-Potassium-Exchanging ATPase
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Galactose