A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae has homology with F0F1 ATP synthase and confers calcium-sensitive growth.
作者： C K Shih , R Wagner , S Feinstein , C Kanik-Ennulat , N Neff
DOI: 10.1128/MCB.8.8.3094
关键词: Biology 、 Calmodulin 、 Saccharomyces cerevisiae 、 Transmembrane domain 、 Mutant 、 ATP synthase 、 Membrane transport 、 Transmembrane protein 、 Trifluoperazine 、 Biochemistry
摘要: The antipsychotic drug trifluoperazine has been long considered a calmodulin inhibitor from in vitro studies but may function vivo as more general by disturbing ion fluxes and altering the membrane potential. Resistance to can arise Saccharomyces cerevisiae cells alterations at least three distinct genetic loci. One locus, defined spontaneous dominant resistance mutation (TFP1-408), was isolated sequenced. sequence of TFP1-408 gene revealed large open reading frame coding for protein 1,031 amino acids with predicted hydrophobic transmembrane domains. A search existing acid sequences significant homology F0F1 ATP synthase. Mutant did not grow efficiently presence 50 mM CaCl2, whereas wild-type did. Wild-type became resistant CaCl2 or MgCl2. showed higher rate calcium transport relative cells. These data suggest that TFP1 product codes ATPase-like enzyme possibly involved Ca2+ generating gradient between two cellular compartments.
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