Chimeras between C. glabrata Cnh1 and S. cerevisiae Nha1 Na+/H+-antiporters are functional proteins increasing the salt tolerance of yeast cells
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Candida glabrata drug effects genetics growth & development metabolism MeSH
- Potassium Chloride pharmacology MeSH
- Sodium Chloride pharmacology MeSH
- Fungal Proteins chemistry genetics metabolism MeSH
- Molecular Sequence Data MeSH
- Sodium-Hydrogen Exchangers chemistry genetics metabolism MeSH
- Cation Transport Proteins chemistry genetics metabolism MeSH
- Recombinant Fusion Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae drug effects genetics growth & development metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Analysis, DNA MeSH
- Sequence Alignment MeSH
- Salt Tolerance * MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Potassium Chloride MeSH
- Sodium Chloride MeSH
- CNH1 protein, Candida albicans MeSH Browser
- Fungal Proteins MeSH
- Sodium-Hydrogen Exchangers MeSH
- NHA1 protein, S cerevisiae MeSH Browser
- Cation Transport Proteins MeSH
- Recombinant Fusion Proteins MeSH
- Saccharomyces cerevisiae Proteins MeSH
The transport activity and substrate specificity of two chimeras consisting of S. cerevisiae Nha1p's N-terminal regions (either first 125 or 184 AA) and the rest of the C. glabrata Cnh1p (up to the total protein length of 946 AA) were compared with those of the two native antiporters. Both chimeric transporters were functional upon expression in S. cerevisiae cells, their presence improved the ability of cells to grow in the presence of high external concentration of K(+), Na(+) or Rb(+) (as chlorides), but not in the presence of the smallest cation (Li(+)). Cation efflux confirmed the ability of chimeras to export cations and showed their significantly reduced transport capacity compared to the wild-type proteins. Despite the very high level of primary sequence identity (87 %) between the S. cerevisiae and C. glabrata plasma-membrane Na(+)/H(+) antiporters, various parts of these proteins are not exchangeable without affecting the antiporter's transport capacity.
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