人类端粒酶包含进化上保守的催化亚基和结构亚基。
Human telomerase contains evolutionarily conserved catalytic and structural subunits.
作者信息
Harrington L, Zhou W, McPhail T, Oulton R, Yeung D S, Mar V, Bass M B, Robinson M O
机构信息
Amgen Institute/Ontario Cancer Institute, Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2C1, Canada.
出版信息
Genes Dev. 1997 Dec 1;11(23):3109-15. doi: 10.1101/gad.11.23.3109.
Abstract
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.
摘要
我们已经克隆并鉴定了一个编码TP2（端粒酶相关蛋白2）的人类基因，该蛋白与逆转录酶以及酿酒酵母和嗜热四膜虫的催化性端粒酶亚基具有相似性。间接免疫荧光显示TP2定位于细胞核。使用针对内源性和表位标记的TP2的抗体，我们发现TP2与人类端粒酶活性以及最近鉴定出的端粒酶相关蛋白TP1特异性相关。TP2逆转录酶结构域内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，端粒酶是一种由结构亚基和催化亚基组成的进化上保守的多亚基复合物。
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