人端粒酶单体的单分子分析

Single-molecule analysis of human telomerase monomer.

作者信息

Alves David, Li Haitao, Codrington Rosalind, Orte Angel, Ren Xiaojun, Klenerman David, Balasubramanian Shankar

机构信息

University Chemical Laboratories, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

出版信息

Nat Chem Biol. 2008 May;4(5):287-9. doi: 10.1038/nchembio.82.

DOI:10.1038/nchembio.82

PMID:18391947

Abstract

Human telomerase is a ribonucleoprotein that is minimally comprised of protein (hTERT) and RNA (hTR) components. We have applied single-molecule fluorescence two-color coincidence detection to characterize complex formation between fluorophore-labeled components in solution. By systematic labeling and in vitro assembly of hTERT, hTR and telomerase's DNA substrate, we have established that catalytically functional human telomerase comprises a stable hTERT:hTR:substrate interaction in a 1:1:1 absolute stoichiometry.

摘要

人类端粒酶是一种核糖核蛋白，最少由蛋白质（hTERT）和RNA（hTR）成分组成。我们应用单分子荧光双色符合检测来表征溶液中荧光团标记成分之间的复合物形成。通过对hTERT、hTR和端粒酶的DNA底物进行系统标记和体外组装，我们确定具有催化功能的人类端粒酶以1:1:1的绝对化学计量比包含稳定的hTERT:hTR:底物相互作用。