Self-assembly of minimal COPII cages
Self-assembly of minimal COPII cages
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DOI：
10.1038/sj.embor.embor812
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发表时间：
2003-04-01
期刊：
影响因子：
7.7
通讯作者：
Orci, L
中科院分区：
文献类型：
--
作者：
Antonny, B;Gounon, P;Orci, L
小G蛋白Sar 1和胞质复合物Sec 23/24和Sec 13/31在内质网膜上依次结合，形成名为COPII的蛋白质外壳，其驱动运输囊泡的形成。使用动态光散射，我们表明，Sec 23/24和Sec 13/31可以在溶液中以化学计量的方式自组装，形成流体动力学半径在40-60 nm范围内的颗粒。通过降低pH、离子强度和/或温度有利于自组装。电子显微镜显示形成了直径为60-120 nm的球形颗粒，其表面上具有紧密的粗糙网格。我们认为，这些结构，这是一个最小的COPII笼，模仿的分子组织的膜相关的COPII外套。
The small G-protein Sar1 and the cytosolic complexes Sec23/24 and Sec13/31 associate sequentially on endoplasmic reticulum membranes to form a protein coat named COPII, which drives the formation of transport vesicles. Using dynamic light scattering, we show that Sec23/24 and Sec13/31 can self-assemble in a stoichiometric manner in solution to form particles with hydrodynamic radii in the range of 40-60 nm. Self-assembly is favoured by lowering the pH, the ionic strength and/or the temperature. Electron microscopy reveals the formation of spherical particles 60-120 nm in diameter with a tight, rough mesh on their surfaces. We suggest that these stuctures, which represent a minimal COPII cage, mimic the molecular organization of the membrane-associated COPII coat.