In Yeast, upc2-1 Confers a Decrease in Tolerance to LiCl and NaCl, Which Can Be Suppressed by the P-Type ATPase Encoded by ENA2
- 1 February 1999
- journal article
- research article
- Published by Mary Ann Liebert Inc in DNA and Cell Biology
- Vol. 18 (2) , 133-139
- https://doi.org/10.1089/104454999315510
Abstract
Wild-type yeast cells are unable to take up sterols from their growth media under aerobic conditions and are relatively resistant to monovalent cations. A yeast mutant (upc2-1) with a defect in the aerobic exclusion of sterols was found to have increased sensitivity to LiCl and NaCl. Although cation sensitivity has been reported for mutants that synthesize altered sterols, the mutant with upc2-1 continues to produce the normal sterol, ergosterol. The ENA2 gene was cloned on the basis of remediating the hypersensitivity to the monovalent cations.Keywords
This publication has 32 references indexed in Scilit:
- Evolution of a Fungal Regulatory Gene Family: The Zn(II)2Cys6 Binuclear Cluster DNA Binding MotifFungal Genetics and Biology, 1997
- PHYSIOLOGICAL IMPLICATIONS OF STEROL BIOSYNTHESIS IN YEASTAnnual Review of Microbiology, 1995
- Isolation and characterization of the Saccharomyces cerevisiae SUT1 gene involved in sterol uptakeGene, 1995
- Mutations in LIS1 (ERG6) gene confer increased sodium and lithium uptake in Saccharomyces cerevisiaeBiochimica et Biophysica Acta (BBA) - Biomembranes, 1994
- Identification and analysis of the Saccharomyces cerevisiae SYR1 gene reveals that ergosterol is involved in the action of syringomycinMicrobiology, 1994
- Improved method for high efficiency transformation of intact yeast cellsNucleic Acids Research, 1992
- A novel P‐type ATPase from yeast involved in sodium transportFEBS Letters, 1991
- Sterol uptake in the yeast, Saccharomyces cerevisiaeBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1983
- Metabolism of Sterols in YeastCRC Critical Reviews in Microbiology, 1978
- Influence of fatty acid and sterol composition on the lipid phase transition and activity of membrane-bound enzymes in Acholeplasma laidlawiiBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973