Nakayama J, Saito M, Nakamura H, Matsuura A, Ishikawa F
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.
Cell. 1997 Mar 21;88(6):875-84. doi: 10.1016/s0092-8674(00)81933-9.
We have cloned and characterized the rat telomerase protein component 1 gene (TLP1), which is related to the gene for Tetrahymena p80. The cDNA encodes a 2629 amino acid sequence and produces the TLP1 proteins p240 and p230. The anti-TLP1 antibody specifically immunoprecipitated the telomerase activity. Moreover, p240 and p230 were copurified with telomerase activity in a series of extensive purification experiments. These results strongly suggest that the TLP1 proteins are components of, or are closely associated with, the rat telomerase. A pulse-chase experiment showed that p240 is modified to p230 in vivo. p230 was the dominant form in telomerase-positive cells, suggesting that modification of the TLP1 protein may regulate telomerase activity in vivo.
我们已经克隆并鉴定了大鼠端粒酶蛋白组分1基因（TLP1），该基因与嗜热四膜虫p80基因相关。cDNA编码一个2629个氨基酸的序列，并产生TLP1蛋白p240和p230。抗TLP1抗体特异性免疫沉淀端粒酶活性。此外，在一系列广泛的纯化实验中，p240和p230与端粒酶活性一起被共纯化。这些结果强烈表明，TLP1蛋白是大鼠端粒酶的组成部分，或与之密切相关。脉冲追踪实验表明，p240在体内被修饰为p230。p230是端粒酶阳性细胞中的主要形式，这表明TLP1蛋白的修饰可能在体内调节端粒酶活性。
