Progress in Human and Tetrahymena Telomerase Structure Determination. Annu Rev Biophys 2017 May 22;46:199-225
Date
03/17/2017Pubmed ID
28301767Pubmed Central ID
PMC5508521DOI
10.1146/annurev-biophys-062215-011140Scopus ID
2-s2.0-85019686968 (requires institutional sign-in at Scopus site) 40 CitationsAbstract
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.
Author List
Chan H, Wang Y, Feigon JAuthor
Yaqiang Wang PhD, MS Assistant Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
HumansModels, Molecular
Protein Domains
Protozoan Proteins
RNA
Telomerase
Tetrahymena
