Zubenko G S, Park F J, Jones E W
Proc Natl Acad Sci U S A. 1983 Jan;80(2):510-4. doi: 10.1073/pnas.80.2.510.
The biosynthesis of carboxypeptidase Y (EC 3.4.16.1) and proteinase A (EC 3.4.23.6) in yeast cells involves a series of posttranslational events, the last of which is dependent upon a function supplied by the PEP4 gene. Because pep4 mutations result in a 90-95% reduction in the levels of activity of at least three additional vacuolar hydrolases, it is likely that these, and perhaps all, yeast vacuolar hydrolases are synthesized as inactive precursors, which mature by a common mechanism that depends upon a function supplied by the PEP4 gene. The pep4 mutation shows an apparent gene dosage effect on levels of activity of proteinases A and B but not on the level of activity of carboxypeptidase Y. This effect appears to come about because the maturation machinery is capable of discriminating among these hydrolase precursors.
酵母细胞中羧肽酶Y（EC 3.4.16.1）和蛋白酶A（EC 3.4.23.6）的生物合成涉及一系列翻译后事件，其中最后一个事件依赖于PEP4基因提供的功能。由于pep4突变导致至少三种其他液泡水解酶的活性水平降低90-95%，因此很可能这些以及或许所有的酵母液泡水解酶都是作为无活性前体合成的，它们通过一种依赖于PEP4基因提供功能的共同机制成熟。pep4突变对蛋白酶A和B的活性水平表现出明显的基因剂量效应，但对羧肽酶Y的活性水平没有影响。这种效应似乎是因为成熟机制能够区分这些水解酶前体。
