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Cation homeostasis in the yeast S. c...
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Withee, Jim Lance.
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Cation homeostasis in the yeast S. cerevisiae.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Cation homeostasis in the yeast S. cerevisiae./
作者:
Withee, Jim Lance.
面頁冊數:
129 p.
附註:
Source: Dissertation Abstracts International, Volume: 60-04, Section: B, page: 1393.
Contained By:
Dissertation Abstracts International60-04B.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9924512
ISBN:
0599240822
Cation homeostasis in the yeast S. cerevisiae.
Withee, Jim Lance.
Cation homeostasis in the yeast S. cerevisiae.
- 129 p.
Source: Dissertation Abstracts International, Volume: 60-04, Section: B, page: 1393.
Thesis (Ph.D.)--Stanford University, 1998.
Calcineurin is a conserved, Ca2+/CaM stimulated protein phosphatase required for Ca2+-dependent signaling in many cell types. In yeast, calcineurin is essential for growth in high concentrations of Na+, Li+, Mn2+, OH - and for maintaining viability during prolonged treatment with mating pheromone. In contrast, the growth of calcineurin-mutant yeast is better than that of wild-type cells in the presence of high concentrations of Ca 2+. We identified mutations that suppress multiple growth defects of calcineurin-deficient yeast (cnb1Delta or cna1 Delta cna2Delta). Mutations in URE2 suppress the sensitivity of calcineurin mutants to Na+, Li+ and Mn2+, and increase their survival during treatment with mating pheromone. ure2 mutations require both the transcription factor Gln3p and the Na+ ATPase Pmr2p to confer Na+ and Li+ tolerance. Mutations in PMA1, which encodes the yeast plasma membrane H+-ATPase, also suppress many growth defects of calcineurin mutants. pma1 mutants display growth phenotypes that are opposite to those of calcineurin mutants; they are resistant to Na+, Li+ and Mn2+ and sensitive to Ca2+. Furthermore, pma1 and calcineurin mutations have antagonistic effects on intracellular [Na+] and [Ca2+]. Finally, we show that yeast expressing a constitutively active allele of calcineurin display pma1-like phenotypes and that membranes from these yeast have decreased levels of Pma1p activity. We also investigated the role of calcineurin in Ca2+ homeostasis. Calcineurin-mutant yeast exhibit an intracellular Ca2+ level approximately 2.5-fold higher than wild-type and show enhanced Ca2+ uptake in response to yeast mating pheromone. Thus, calcineurin has an inhibitory affect on Ca 2+ accumulation during growth under standard conditions as well as on both the magnitude and sensitivity of the mating pheromone-induced Ca 2+ signal in yeast. These studies further characterize the roles that URE2, PMA1 and calcineurin play in regulating intracellular ion homeostasis.
ISBN: 0599240822Subjects--Topical Terms:
1017686
Biology, Cell.
Cation homeostasis in the yeast S. cerevisiae.
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Calcineurin is a conserved, Ca2+/CaM stimulated protein phosphatase required for Ca2+-dependent signaling in many cell types. In yeast, calcineurin is essential for growth in high concentrations of Na+, Li+, Mn2+, OH - and for maintaining viability during prolonged treatment with mating pheromone. In contrast, the growth of calcineurin-mutant yeast is better than that of wild-type cells in the presence of high concentrations of Ca 2+. We identified mutations that suppress multiple growth defects of calcineurin-deficient yeast (cnb1Delta or cna1 Delta cna2Delta). Mutations in URE2 suppress the sensitivity of calcineurin mutants to Na+, Li+ and Mn2+, and increase their survival during treatment with mating pheromone. ure2 mutations require both the transcription factor Gln3p and the Na+ ATPase Pmr2p to confer Na+ and Li+ tolerance. Mutations in PMA1, which encodes the yeast plasma membrane H+-ATPase, also suppress many growth defects of calcineurin mutants. pma1 mutants display growth phenotypes that are opposite to those of calcineurin mutants; they are resistant to Na+, Li+ and Mn2+ and sensitive to Ca2+. Furthermore, pma1 and calcineurin mutations have antagonistic effects on intracellular [Na+] and [Ca2+]. Finally, we show that yeast expressing a constitutively active allele of calcineurin display pma1-like phenotypes and that membranes from these yeast have decreased levels of Pma1p activity. We also investigated the role of calcineurin in Ca2+ homeostasis. Calcineurin-mutant yeast exhibit an intracellular Ca2+ level approximately 2.5-fold higher than wild-type and show enhanced Ca2+ uptake in response to yeast mating pheromone. Thus, calcineurin has an inhibitory affect on Ca 2+ accumulation during growth under standard conditions as well as on both the magnitude and sensitivity of the mating pheromone-induced Ca 2+ signal in yeast. These studies further characterize the roles that URE2, PMA1 and calcineurin play in regulating intracellular ion homeostasis.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9924512
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