Heuser J E, Keen J H, Amende L M, Lippoldt R E, Prasad K
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
J Cell Biol. 1987 Nov;105(5):1999-2009. doi: 10.1083/jcb.105.5.1999.
It has recently been reported that 8S clathrin trimers or "triskelions" form larger 27S oligomers upon dialysis into low ionic strength buffers (Prasad, K., R. E. Lippoldt, H. Edelhoch, and M. S. Lewis, 1986, Biochemistry, 25:5214-5219). Here, deep-etch electron microscopy of the 27S species reveals that they are closed tetrahedra composed of four clathrin triskelions. This was determined by two approaches. First, standard quick-freezing and freeze-etching of unfixed 27S species suspended in 2 mM 2-(N-morpholino)ethane sulfonic acid (MES) buffer, pH 5.9, yielded unambiguous images of tetrahedra that measured 33 nm on each edge. Second, the technique of freeze-drying molecules on mica (Heuser, J. E., 1983, J. Mol. Biol., 169:155-195) was modified to overcome the low affinity of mica in 2 mM MES, by pretreating the mica with polylysine. Thereafter, 27S species adsorbed avidly to it and collapsed into characteristic configurations containing four globular domains, each linked to the others by three approximately 33-nm struts. The globular domains look like vertices of deep-etched clathrin triskelions and the links, numbering 12 in all, look like four sets of triskelion legs. New light scattering and equilibrium centrifugation data confirm that 27S polymer is four times as massive as one clathrin triskelion. We conclude that in conditions that do not favor the formation of standard clathrin cages, low affinity interactions lead to closed, symmetrical assemblies of four triskelions, each of which assumes a unique puckered, straight-legged configuration to create the edges of a tetrahedron. Tetrahedra are similar in construction to the cubic octomers of clathrin recently found in ammonium sulfate solutions (Sorger, P. K., R. A. Crowther, J. T. Finch, and B. M. F. Pearse, 1986, J. Cell Biol., 103:1213-1219) but are still smaller, involving only half as many clathrin triskelions.
最近有报道称,8S网格蛋白三聚体或“三脚蛋白复合体”在透析到低离子强度缓冲液中时会形成更大的27S寡聚体(普拉萨德,K.,R. E. 利波尔特,H. 埃德尔霍赫,和M. S. 刘易斯,1986,《生物化学》,25:5214 - 5219)。在此,对27S物种的深度蚀刻电子显微镜观察表明,它们是由四个网格蛋白三脚蛋白复合体组成的封闭四面体。这是通过两种方法确定的。首先,对悬浮在pH 5.9的2 mM 2 -(N - 吗啉代)乙烷磺酸(MES)缓冲液中的未固定27S物种进行标准的快速冷冻和冷冻蚀刻,得到了清晰的四面体图像,每条边的长度为33 nm。其次,对在云母上冷冻干燥分子的技术(休泽尔,J. E.,1983,《分子生物学杂志》,169:155 - 195)进行了改进,通过用聚赖氨酸预处理云母来克服云母在2 mM MES中的低亲和力。此后,27S物种 avidly吸附到它上面,并坍塌成包含四个球状结构域的特征构型,每个球状结构域通过三个约33 nm的支柱与其他结构域相连。球状结构域看起来像深度蚀刻的网格蛋白三脚蛋白复合体的顶点,而连接结构总共12个,看起来像四组三脚蛋白复合体的腿。新的光散射和平衡离心数据证实,27S聚合物的质量是一个网格蛋白三脚蛋白复合体的四倍。我们得出结论,在不利于形成标准网格蛋白笼的条件下,低亲和力相互作用导致四个三脚蛋白复合体形成封闭、对称的组装体,每个三脚蛋白复合体呈现出独特的褶皱、直腿构型,以形成四面体的边缘。四面体的结构与最近在硫酸铵溶液中发现的网格蛋白立方八聚体(索尔格,P. K.,R. A. 克劳瑟,J. T. 芬奇,和B. M. F. 皮尔斯,1986,《细胞生物学杂志》,103:1213 - 1219)相似,但仍然较小,只涉及一半数量的网格蛋白三脚蛋白复合体。