Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 Feb;23(2):175–188. doi: 10.1261/rna.058743.116

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2017 Parks et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

PMC Copyright notice

FIGURE 1. — Single-molecule FRET network in the active telomerase RNP. (A) A simplified catalytic mechanism of telomerase is delineated. Telomerase binds to a DNA substrate and reverse transcribes the integral RNA template. The nascent DNA is realigned with the downstream template region, allowing addition of a subsequent telomere repeat to the DNA substrate. (B) Secondary structures of core and CR4/5 domains used in telomerase reconstitution. Five label sites (denoted by black circles) span the two domains and create a network of FRET pairs. Secondary structure information was adapted from the telomerase database (Podlevsky et al. 2008). (C) Dye-labeled RNA fragments are reconstituted with TERT to generate catalytically active RNPs. Each complex is surface immobilized through a 5′ biotinylated DNA primer (TG)₆TTAGGG that hybridizes to the template region of telomerase RNA.