Structural biology of telomerase and its interaction at telomeres

被引：25

作者：

Wang, Yaqiang ^{[1
]}

Feigon, Juli ^{[1
]}

机构：

[1] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2017年 / 47卷

基金：

美国国家科学基金会;

关键词：

TEMPLATE-BOUNDARY DEFINITION; N-TERMINAL DOMAIN; GROUP-II INTRON; TETRAHYMENA TELOMERASE; SINGLE-MOLECULE; REVERSE-TRANSCRIPTASE; RNA PSEUDOKNOT; YEAST TELOMERASE; FINGERS DOMAIN; DNA-SYNTHESIS;

D O I：

10.1016/j.sbi.2017.06.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Telomerase is an RNP that synthesizes the 3' ends of linear chromosomes and is an important regulator of telomere length. It contains a single long non-coding telomerase RNA (TER), telomerase reverse transcriptase (PERT), and other proteins that vary among organisms. Recent progress in structural biology of telomerase includes reports of the first cryo-electron microscopy structure of telomerase, from Tetrahymena, new crystal structures of TERT domains, telomerase RNA structures and models, and identification in Tetrahymena telomerase holoenzyme of human homologues of telomere-associated proteins that have provided a more unified view of telomerase interaction at telomeres as well as insights into the role of telomerase RNA in activity and assembly.

引用

页码：77 / 87

页数：11

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