PREVENTION OF RAPID INTRACELLULAR DEGRADATION OF ODC BY A CARBOXYL-TERMINAL TRUNCATION
PREVENTION OF RAPID INTRACELLULAR DEGRADATION OF ODC BY A CARBOXYL-TERMINAL TRUNCATION
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DOI：
10.1126/science.2928784
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发表时间：
1989-03-17
期刊：
影响因子：
56.9
通讯作者：
COFFINO, P
中科院分区：
文献类型：
--
作者：
GHODA, L;WETTERS, TV;COFFINO, P
鸟氨酸脱羧酶(ODC)通过截短其羧基末端的37个残基，从哺乳动物细胞内半衰期较短的蛋白质转变为稳定的蛋白质。表达Will-type蛋白的细胞失去ODC活性，半衰期约为1小时。然而，表达截短蛋白的细胞至少在4小时内保持了全部活性。免疫沉淀法和凝胶电泳法的脉冲追逐实验证实了截短的稳定作用。因此，一个羧基末端结构域是导致小鼠ODC在细胞内快速降解的原因。
Ornithine decarboxylase (ODC) was converted from a protein with a short intracellular half-life in mammalian cells to a stable protein by truncating 37 residues at its carboxyl terminus. Cells expressing will-type protein lost ODC activity with a half-life of approximately 1 hour. Cells expressing the truncated protein, however, retained full activity for at least 4 hours. Pulse-chase experiments in which immunoprecipitation and gel electrophoresis were used confirmed the stabilizing effect of the truncation. Thus, a carboxyl-terminal domain is responsible for the rapid intracellular degradation of murine ODC.