Exploration of yeast alkali metal cation/H+ antiporters: sequence and structure comparison
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17176761
DOI
10.1007/bf02931585
Knihovny.cz E-resources
- MeSH
- DNA, Fungal analysis MeSH
- Potassium-Hydrogen Antiporters chemistry classification genetics MeSH
- Phylogeny MeSH
- Membrane Proteins chemistry classification genetics MeSH
- Molecular Sequence Data MeSH
- Sodium-Hydrogen Exchangers chemistry classification genetics MeSH
- Cation Transport Proteins chemistry classification genetics MeSH
- Saccharomyces cerevisiae Proteins chemistry classification genetics MeSH
- Amino Acid Sequence MeSH
- Sequence Analysis, DNA MeSH
- Sequence Homology, Amino Acid MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- DNA, Fungal MeSH
- Potassium-Hydrogen Antiporters MeSH
- KHA1 protein, S cerevisiae MeSH Browser
- Membrane Proteins MeSH
- Sodium-Hydrogen Exchangers MeSH
- NHA1 protein, S cerevisiae MeSH Browser
- NHX1 protein, S cerevisiae MeSH Browser
- Cation Transport Proteins MeSH
- Saccharomyces cerevisiae Proteins MeSH
The Saccharomyces cerevisiae genome contains three genes encoding alkali metal cation/H+ antiporters (Nha1p, Nhx1p, Kha1p) that differ in cell localization, substrate specificity and physiological function. Systematic genome sequencing of other yeast species revealed highly conserved homologous ORFs in all of them. We compared the yeast sequences both at DNA and protein levels. The subfamily of yeast endosomal/prevacuolar Nhx1 antiporters is closely related to mammalian plasma membrane NHE proteins and to both plasma membrane and vacuolar plant antiporters. The high sequence conservation within this subfamily of yeast antiporters suggests that Nhx1p is of great importance in cell physiology. Yeast Kha1 proteins probably belong to the same subfamily as bacterial antiporters, whereas Nhal proteins form a distinct subfamily.
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