Gong F C, Giddings T H, Meehl J B, Staehelin L A, Galbraith D W
Department of Plant Sciences, University of Arizona, Tucson, 85721, USA.
Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2219-23. doi: 10.1073/pnas.93.5.2219.
We have expressed a fusion protein formed between the avian infectious bronchitis virus M protein and the bacterial enzyme beta-glucuronidase in transgenic tobacco cells. Electron microscope images of such cells demonstrate that overexpression of this fusion protein gives rise to a type of endoplasmic reticulum membrane domain in which adjacent membranes become zippered together apparently as a consequence of the oligomerizing action of beta-glucuronidase. These zippered (Z-) membranes lack markers of the endoplasmic reticulum (NADH cytochrome c reductase and ribosomes) and accumulate in the cells in the form of multilayered scroll-like structures (up to 2 micrometers in diameter; 20-50 per cell) without affecting plant growth. The discovery of Z-membranes has broad implications for biology and biotechnology in that they provide a means for accumulating large quantities of recombinant membrane proteins within discrete domains of native membranes.
我们已在转基因烟草细胞中表达了一种由禽传染性支气管炎病毒M蛋白与细菌酶β-葡萄糖醛酸酶形成的融合蛋白。此类细胞的电子显微镜图像显示,这种融合蛋白的过表达会产生一种内质网膜结构域,其中相邻的膜显然由于β-葡萄糖醛酸酶的寡聚作用而拉链式地结合在一起。这些拉链式(Z-)膜缺乏内质网标记物(NADH细胞色素c还原酶和核糖体),并以多层涡卷状结构(直径可达2微米;每个细胞20 - 50个)的形式在细胞中积累,且不影响植物生长。Z-膜的发现对生物学和生物技术具有广泛影响,因为它们提供了一种在天然膜的离散结构域内积累大量重组膜蛋白的方法。