https://scholars.lib.ntu.edu.tw/handle/123456789/188293
標題: | Functional Characterization and Localization of Acetyl-Coa Hydrolase, Ach 1p, in Saccharomyces Cerevisiae | 作者: | CHEN, YEE-CHUN | 關鍵字: | COENZYME-A HYDROLASE;AMINO-ACID-SEQUENCE;RAT-LIVER;ACETATE UTILIZATION;FILAMENTOUS GROWTH;PROTEIN IMPORT | 公開日期: | 2003 | 卷: | v.278 | 期: | n.19 | 起(迄)頁: | 17203-17209 | 來源出版物: | JOURNAL OF BIOLOGICAL CHEMISTRY | 摘要: | Acetyl-CoA hydrolase (Ach1p), catalyzing the hydrolysis of acetyl-CoA, is presumably involved in regulating intracellular acetyl-CoA or CoASH pools ; however, its intracellular functions and distribution remain to be established. Using site-directed mutagenesis analysis, we demonstrated that the enzymatic activity of Ach1p is dependent upon its putative acetyl -CoA binding sites. The ach1 mutant causes a growth defect in acetate but not in other non-fermentable carbon sources, suggesting that Ach1p is not involved in mitochondrial biogenesis. Overexpression of Ach1p, but not constructs containing acetyl-CoA binding site mutations, in ach1-1 complemented the defect of acetate utilization. By subcellular fractionation, most of the Ach1 p in yeast was distributed with mitochondria and little Ach 1 p in the cytoplasm. By immunofluorescence microscopy, we show that Ach1p and acetyl-CoA binding site-mutated constructs, but not its N-terminal deleted construct, are localized in mitochondria. Moreover, the onset of pseudohyphal development in homozygote ach1-1 diploids was abolished. We infer that Ach1p may be involved in a novel acetyl-CoA biogenesis and/or acetate utilization in mitochondria and thereby indirectly affect pseudohyphal development in yeast. |
URI: | http://ntur.lib.ntu.edu.tw//handle/246246/95241 |
顯示於: | 醫學系 |
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