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Progress in Human and Tetrahymena Telomerase Structure Determination.
Annual Review of Biophysics ( IF 10.4 ) Pub Date : 2017-05-22 00:00:00 , DOI: 10.1146/annurev-biophys-062215-011140
Henry Chan 1 , Yaqiang Wang 1 , Juli Feigon 1
Affiliation  

Telomerase is an RNA–protein complex that extends the 3′ ends of linear chromosomes, using a unique telomerase reverse transcriptase (TERT) and template in the telomerase RNA (TR), thereby helping to maintain genome integrity. TR assembles with TERT and species-specific proteins, and telomerase function in vivo requires interaction with telomere-associated proteins. Over the past two decades, structures of domains of TR and TERT as well as other telomerase- and telomere-interacting proteins have provided insights into telomerase function. A recently reported 9-Å cryo–electron microscopy map of the Tetrahymena telomerase holoenzyme has provided a framework for understanding how TR, TERT, and other proteins from ciliate as well as vertebrate telomerase fit and function together as well as unexpected insight into telomerase interaction at telomeres. Here we review progress in understanding the structural basis of human and Tetrahymena telomerase activity, assembly, and interactions.

中文翻译:



人类和四膜虫端粒酶结构测定的进展。



端粒酶是一种 RNA-蛋白质复合物,它使用独特的端粒酶逆转录酶 (TERT) 和端粒酶 RNA (TR) 中的模板来延伸线性染色体的 3' 端,从而有助于维持基因组完整性。 TR 与 TERT 和物种特异性蛋白组装,体内端粒酶功能需要与端粒相关蛋白相互作用。在过去的二十年中,TR 和 TERT 以及其他端粒酶和端粒相互作用蛋白的结构域结构为我们提供了对端粒酶功能的深入了解。最近报道的四膜虫端粒酶全酶的 9 Å 冷冻电子显微镜图为理解 TR、TERT 和其他来自纤毛虫和脊椎动物端粒酶的蛋白质如何配合和发挥作用提供了一个框架,并为端粒酶相互作用提供了意想不到的见解。端粒。在这里,我们回顾了理解人类和四膜虫端粒酶活性、组装和相互作用的结构基础的进展。

更新日期:2017-05-22
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