Univalent cation fluxes in yeast
Jazyk angličtina Země Velká Británie, Anglie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
9530519
DOI
10.1080/15216549800201382
Knihovny.cz E-zdroje
- MeSH
- draslík metabolismus MeSH
- fungální proteiny genetika fyziologie MeSH
- glukosa farmakologie MeSH
- inhibitory enzymů MeSH
- iontový transport MeSH
- kationty jednomocné metabolismus MeSH
- membránové proteiny genetika fyziologie MeSH
- mutace MeSH
- proteiny přenášející kationty * MeSH
- protonové ATPasy antagonisté a inhibitory MeSH
- protony MeSH
- rubidium metabolismus MeSH
- Saccharomyces cerevisiae - proteiny * MeSH
- Saccharomyces cerevisiae genetika metabolismus MeSH
- thallium metabolismus MeSH
- transportní proteiny genetika fyziologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- draslík MeSH
- fungální proteiny MeSH
- glukosa MeSH
- inhibitory enzymů MeSH
- kationty jednomocné MeSH
- membránové proteiny MeSH
- proteiny přenášející kationty * MeSH
- protonové ATPasy MeSH
- protony MeSH
- rubidium MeSH
- Saccharomyces cerevisiae - proteiny * MeSH
- thallium MeSH
- transportní proteiny MeSH
- TRK1 protein, S cerevisiae MeSH Prohlížeč
- TRK2 protein, S cerevisiae MeSH Prohlížeč
Transport of H+, K+, Rb+ and Tl+ ions was studied in a wild-type strain of Saccharomyces cerevisiae and in its mutants defective in the high-affinity K+ transport system TRK1 and in the double mutant with an additional deletion in the TRK2 gene. In the absence of glucose K+, Rb+ and Tl+ elicited a more or less stoichiometric exchange outflow of H+, in the mutants K+ moved out of cells even in the presence of 10 mM KCl or KNO3. In the presence of glucose in the wild type, K+, Rb+ and Tl+ brought about a massive outflow of H+ while being transported inward against high concentration gradients. In the trk1 delta mutant the exchange fluxes were reduced by 65-85%, in the double mutant those of K+, Rb+ and Tl+ practically cease but outflow of H+ caused by Tl+ remained at the level of the trk1 delta mutant. It appears that, in addition to the H+ export by the PMA1-coded plasma membrane H(+)-ATPase, at least three different univalent-cation involving activities are present: the high-affinity transport system for K+ (TRK1), another system (possibly TRK2) with different responses to K+ and Rb+, vs. Tl+, and an active system for K+ export. The first two are apparently active exchange systems for K+, Rb+, and Tl+ against H+. The source of energy for these highly active transports (acting against gradients of 1000:1 and 5000:1, respectively) is unclear.
Citace poskytuje Crossref.org
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