Gerich B, Orci L, Tschochner H, Lottspeich F, Ravazzola M, Amherdt M, Wieland F, Harter C
Institut für Biochemie I, Heidelberg, Germany.
Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3229-33. doi: 10.1073/pnas.92.8.3229.
To complete the molecular characterization of coatomer, the preformed cytosolic complex that is involved in the formation of biosynthetic transport vesicles, we have cloned and characterized the gene for non-clathrin-coat protein alpha (alpha-COP) from Saccharomyces cerevisiae. The derived protein, molecular weight of 135,500, contains four WD-40 repeated motifs (Trp/Asp-containing motifs of approximately 40 amino acids). Disruption of the yeast alpha-COP gene is lethal. Comparison of the DNA-derived primary structure with peptides from bovine alpha-COP shows a striking homology. alpha-COP is localized to coated transport vesicles and coated buds of Golgi membranes derived from CHO cells.
为了完成对参与生物合成运输小泡形成的预先形成的胞质复合物——衣被蛋白复合体的分子特性分析，我们从酿酒酵母中克隆并鉴定了非网格蛋白衣被蛋白α（α-COP）的基因。推导的蛋白质分子量为135,500，包含四个WD-40重复基序（含约40个氨基酸的色氨酸/天冬氨酸基序）。酵母α-COP基因的破坏是致死性的。将DNA推导的一级结构与来自牛α-COP的肽进行比较，显示出显著的同源性。α-COP定位于源自CHO细胞的高尔基体膜的被膜运输小泡和被膜芽上。
