Silver P A, Keegan L P, Ptashne M
Proc Natl Acad Sci U S A. 1984 Oct;81(19):5951-5. doi: 10.1073/pnas.81.19.5951.
We have studied the intracellular compartmentalization in yeast of Escherichia coli beta-galactosidase bearing heterologous amino acid sequences at its amino terminus. Chimeras containing as few as 74 NH2-terminal amino acids of GAL4, a yeast positive regulatory protein, at the amino terminus accumulate in the cell nucleus. This and other results are consistent with the proposal that the GAL4 gene product mediates positive control by binding to DNA and that the information for nuclear localization resides in its amino terminus. The amino acid sequence of the GAL4 amino terminus does not agree with the previously proposed consensus sequences responsible for nuclear localization. The beta-galactosidase activity in cells bearing the non-nuclear chimeric proteins is 10-fold greater than in cells bearing chimeric proteins that specifically concentrate in the nucleus.
我们研究了在其氨基末端带有异源氨基酸序列的大肠杆菌β-半乳糖苷酶在酵母中的细胞内区室化。在氨基末端含有低至74个酵母阳性调节蛋白GAL4的NH2-末端氨基酸的嵌合体聚集在细胞核中。这一结果以及其他结果与以下观点一致：GAL4基因产物通过与DNA结合介导正调控，并且核定位信息存在于其氨基末端。GAL4氨基末端的氨基酸序列与先前提出的负责核定位的共有序列不一致。携带非核嵌合蛋白的细胞中的β-半乳糖苷酶活性比携带特异性集中在细胞核中的嵌合蛋白的细胞中的活性高10倍。
