de Hostos E L, Bradtke B, Lottspeich F, Gerisch G
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Cell Motil Cytoskeleton. 1993;26(3):181-91. doi: 10.1002/cm.970260302.
A 17 kDa protein, designated as coactosin, has been purified from an actin-myosin complex reconstituted in vitro from a soluble fraction of Dictyostelium discoideum cells. The protein binds to F-actin in vitro without significantly altering its viscosity. Immunoblots labeled with monoclonal antibodies indicate that part of the protein is associated with the detergent-insoluble cytoskeleton. cDNA clones comprising the entire coding region of coactosin have been isolated from an expression library. The cDNA-derived amino-acid sequence reveals similarities of coactosin to the drebrins identified in neurons and to actin-binding proteins from other organisms, including yeast ABP1p, and yeast and vertebrate cofilins.
一种名为共肌动蛋白的17 kDa蛋白质,已从用盘基网柄菌细胞可溶部分体外重构的肌动蛋白-肌球蛋白复合物中纯化出来。该蛋白质在体外与F-肌动蛋白结合,而不会显著改变其黏度。用单克隆抗体标记的免疫印迹表明,该蛋白质的一部分与去污剂不溶性细胞骨架相关。已从一个表达文库中分离出包含共肌动蛋白完整编码区的cDNA克隆。cDNA推导的氨基酸序列显示,共肌动蛋白与在神经元中鉴定出的脑桥蛋白以及来自其他生物体(包括酵母ABP1p、酵母和脊椎动物的丝切蛋白)的肌动蛋白结合蛋白具有相似性。