SYNTHESIS AND MATURATION OF THE YEAST VACUOLAR ENZYMES CARBOXYPEPTIDASE Y AND AMINOPEPTIDASE-I
SYNTHESIS AND MATURATION OF THE YEAST VACUOLAR ENZYMES CARBOXYPEPTIDASE Y AND AMINOPEPTIDASE-I
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DOI：
10.1016/0167-4781(83)90019-2
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发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
JONES, EW
中科院分区：
文献类型：
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作者：
DISTEL, B;AL, EJM;JONES, EW
两种液泡酶羧肽酶Y和氨肽酶I分别来自于S.研究了酿酒酵母的生物合成、成熟和从其合成位点转移到细胞器中。这2种蛋白质的可翻译mRNA水平在以葡萄糖作为C源的指数生长期结束时增加超过10倍，并在稳定期再次降低。通过[35 S]甲硫氨酸体内脉冲标记鉴定了羧肽酶Y的两种前体。如衣霉素对N-连接糖基化的抑制所示，它们的碳水化合物量不同。第一种是表观分子量为67 kDa [千道尔顿]的蛋白质，它可以通过69 kDa的中间体转化为成熟的60 kDa蛋白质。在pep 4 -3突变体中，其在几种液泡酶的成熟中受到干扰（Hemmings等，1981），69-kDa前体在液泡中积累。羧肽酶Y最后的蛋白水解裂解显然可以发生在液泡中。
The 2 vacuolar enzymes carboxypeptidase Y and aminopeptidase I from S. cerevisiae were studied with respect to biosynthesis, maturation and transfer from their site of synthesis into the organelle. The levels of translatable mRNA for these 2 proteins increase more than 10-fold at the end of the exponential growth period on glucose as C source and decrease again in the stationary phase. Two precursors of carboxypeptidase Y were identified by in vivo pulse-labeling with [35S]methionine. These differ in their amount of carbohydrate as shown by inhibition of N-linked glycosylation with tunicamycin. The 1st is a protein with an apparent MW of 67 kDa [kilodalton], which can be converted into the mature 60-kDa protein via an intermediate of 69 kDa. In the pep4-3 mutant, which is disturbed in the maturation of several vacuolar enzymes (Hemmings, et al. 1981), the 69-kDa precursor accumulates in the vacuole. The final proteolytic cleavage of carboxypeptidase Y can apparently occur in the vacuole.