Rice Na+/H+-antiporter Nhx1 partially complements the alkali-metal-cation sensitivity of yeast strains lacking three sodium transporters
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
15702539
DOI
10.1007/bf02931527
Knihovny.cz E-zdroje
- MeSH
- DNA rostlinná genetika MeSH
- geny hub MeSH
- kovy metabolismus farmakologie MeSH
- mutace MeSH
- Na(+)-H(+) antiport genetika metabolismus MeSH
- rekombinantní proteiny genetika metabolismus MeSH
- rostlinné geny MeSH
- rýže (rod) genetika metabolismus MeSH
- Saccharomyces cerevisiae - proteiny genetika metabolismus MeSH
- Saccharomyces cerevisiae účinky léků genetika metabolismus MeSH
- sekvence nukleotidů MeSH
- testy genetické komplementace MeSH
- vakuoly metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- DNA rostlinná MeSH
- kovy MeSH
- Na(+)-H(+) antiport MeSH
- rekombinantní proteiny MeSH
- Saccharomyces cerevisiae - proteiny MeSH
A triple mutant strain of Saccharomyces cerevisiae lacking its own Na+-ATPases and Na+/H+ antiporters (enal-4delta nha1delta nhx1delta) was used for the expression of the Oryza sativa NHX1 gene encoding a putative vacuolar Na+/H+ exchanger. Upon expression in yeast cells, the OsNhx 1p is not a transport system specific only for sodium cations but it has a broad substrate specificity for at least four alkali metal cations (Na+, Li+, K+ and Rb+) and is able to substitute for the endogenous yeast ScNhx1 antiporter. Its activity contributes to sequestration of alkali metal cations in intracellular vesicles.
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Exploration of yeast alkali metal cation/H+ antiporters: sequence and structure comparison
