Lee G, Neve R L, Kosik K S
Department of Neurology (Neuroscience), Harvard Medical School, Brigham and Women's Hospital, Boston, Massachusetts 02115.
Neuron. 1989 Jun;2(6):1615-24. doi: 10.1016/0896-6273(89)90050-0.
Tau protein is a microtubule-associated protein implicated in the spatial and temporal specification of microtubules and has been found in the neurofibrillary tangles of Alzheimer's disease. Determination of tau protein structure has revealed three 18 amino acid repeated sequences hypothesized to be tubulin binding sites. Using tau cDNA clones from human fetal brain, we employed E. coli expression systems to synthesize tau protein and fragments of tau protein in order to identify the microtubule binding site. A fragment containing the three repeated sequences binds microtubules, while the amino-terminal half of the protein does not bind. Fragments containing two or one repeat are also capable of binding, indicating that the basic tubulin interacting unit is one repeat.
tau蛋白是一种与微管相关的蛋白，涉及微管的空间和时间特异性，并且已在阿尔茨海默病的神经原纤维缠结中被发现。tau蛋白结构的测定揭示了三个18个氨基酸的重复序列，推测它们是微管蛋白结合位点。利用来自人类胎儿大脑的tau cDNA克隆，我们采用大肠杆菌表达系统来合成tau蛋白和tau蛋白片段，以便鉴定微管结合位点。一个包含三个重复序列的片段能结合微管，而该蛋白的氨基末端一半则不能结合。包含两个或一个重复序列的片段也能够结合，这表明基本的微管蛋白相互作用单元是一个重复序列。
