Harrington Lea
Department of Medical Biophysics, Ontario Cancer Institute, University of Toronto, 620 University Avenue, Rm. 932, Ontario M5G 2C1, Toronto, Canada.
Cancer Lett. 2003 May 15;194(2):139-54. doi: 10.1016/s0304-3835(02)00701-2.
Arthur Kornberg "never met a dull enzyme" (For the Love of Enzymes: The Odyssey of a Biochemist, Harvard University Press, 1989) and telomerase is no exception. Telomerase is a remarkable polymerase that uses an internal RNA template to reverse-transcribe telomere DNA, one nucleotide at a time, onto telomeric, G-rich single-stranded DNA. In the 17 years since its discovery, the characterization of telomerase enzyme components has uncovered a highly conserved family of telomerase reverse transcriptases that, together with the telomerase RNA, appear to comprise the enzymatic core of telomerase. While not as comprehensively understood as yet, some telomerase-associated proteins also serve crucial roles in telomerase function in vivo, such as telomerase ribonudeoprotein (RNP) assembly, recruitment to the telomere, and the coordination of DNA replication at the telomere. A selected overview of the biochemical properties of this unique enzyme, in vitro and in vivo, will be presented.
亚瑟·科恩伯格曾说“从未遇到过无趣的酶”(《对酶的热爱:一位生物化学家的奥德赛》,哈佛大学出版社,1989年),端粒酶也不例外。端粒酶是一种非凡的聚合酶,它利用内部RNA模板将端粒DNA逐个核苷酸地逆转录到富含G的端粒单链DNA上。自发现端粒酶的17年来,对端粒酶酶成分的表征揭示了一个高度保守的端粒酶逆转录酶家族,它们与端粒酶RNA一起,似乎构成了端粒酶的酶核心。虽然目前尚未得到全面了解,但一些端粒酶相关蛋白在端粒酶的体内功能中也起着关键作用,如端粒酶核糖核蛋白(RNP)组装、招募到端粒以及端粒处DNA复制的协调。本文将对这种独特酶在体外和体内的生化特性进行简要概述。