Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein

摘要

端粒酶(起稳定线形染色体端部这一重要作用的核糖核蛋白(RNF·)组 合体)的生物起源是一个健康细胞中的一个重要过程，破坏它们的突 变能引起疾病。研究人员对RNP组合体的机制很不了解。Michael Stone等人利用一种单分子方法对端粒酶组合体进行了实时分析，对 每个组合步骤的精确顺序进行了分解。他们的结果确定了一个分成不 同层次的组合机制，该机制包含两个连续的步骤一由蛋白诱导的RNA 折叠，最后是将端粒酶复合物模制成它的功能形状。%Telomerase is an essential cellular ribonucleoprotein (RNP) that solves the end replication problem and maintains chromosome stability by adding telomeric DNA to the termini of linear chromosomes. Genetic mutations that abrogate the normal assembly of telomerase RNP cause human disease. It is therefore of fundamental and medical importance to decipher cellular strategies for telomerase biogenesis, which will require new insights into how specific interactions occur in a precise order along the RNP assembly pathway.