Human telomerase contains evolutionarily conserved catalytic and structural subunits
Human telomerase contains evolutionarily conserved catalytic and structural subunits
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DOI：
10.1101/gad.11.23.3109
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发表时间：
1997-12-01
影响因子：
10.5
通讯作者：
Robinson, MO
中科院分区：
文献类型：
--
作者：
Harrington, L;Zhou, W;Robinson, MO
我们已经克隆并鉴定了编码TP2（端粒酶相关蛋白2）的人类基因，TP2是一种类似于酿酒酵母（Saccharomyces cerevisiae）和羽状游仆虫（Euplotes aediculatus）的逆转录酶和催化端粒酶亚基的蛋白质。间接免疫荧光显示TP 2定位于细胞核。使用内源性和表位标记的TP2抗体，我们发现TP2与人端粒酶活性和最近鉴定的端粒酶相关蛋白TP1特异性相关。TP2逆转录酶结构域中保守残基的突变严重降低了相关的端粒酶活性。这些结果表明，端粒酶是一个进化上保守的多亚基复合体，由结构亚基和催化亚基组成。
We have cloned and characterized a human gene encoding TP2 (telomerase-associated protein 2), a protein with similarity to reverse transcriptases and the catalytic telomerase subunits from Saccharomyces cerevisiae and Euplotes aediculatus. Indirect immunofluorescence revealed that TP2 was localized to the nucleus. Using antibodies to endogenous and epitope-tagged TP2, we found that TP2 was associated specifically with human telomerase activity and the recently identified telomerase-associated protein TP1. Mutation of conserved residues within the reverse transcriptase domain of TP2 severely reduced associated telomerase activity. These results suggest that telomerase is an evolutionarily conserved multisubunit complex composed of both structural and catalytic subunits.