Analysis of Telomerase RNA Structure in Physcomitrium patens Indicates Functionally Relevant Transitions Between OPEN and CLOSED Conformations
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
38143018
DOI
10.1016/j.jmb.2023.168417
PII: S0022-2836(23)00534-X
Knihovny.cz E-resources
- Keywords
- DMS-Map Seq, RNA secondary structure, SHAPE-Map Seq, single molecule analysis, telomerase RNA,
- MeSH
- Nucleic Acid Conformation MeSH
- Bryopsida * MeSH
- RNA * chemistry genetics MeSH
- Telomerase * chemistry genetics MeSH
- Single Molecule Imaging MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- RNA * MeSH
- Telomerase * MeSH
- telomerase RNA MeSH Browser
Telomerase RNA (TR) conformation determines its function as a template for telomere synthesis and as a scaffold for the assembly of the telomerase nucleoprotein complex. Experimental analyses of TR secondary structure using DMS-Map Seq and SHAPE-Map Seq techniques show its CLOSED conformation as the consensus structure where the template region cannot perform its function. Our data show that the apparent discrepancy between experimental results and predicted TR functional conformation, mostly ignored in published studies, can be explained using data analysis based on single-molecule structure prediction from individual sequencing reads by the recently established DaVinci method. This method results in several clusters of secondary structures reflecting the structural dynamics of TR, possibly related to its multiple functional states. Interestingly, the presumed active (OPEN) conformation of TR corresponds to a minor fraction of TR under in vivo conditions. Therefore, structural polymorphism and dynamic TR transitions between CLOSED and OPEN conformations may be involved in telomerase activity regulation as a switch that functions independently of total TR transcript levels.
References provided by Crossref.org
Characterisation of the Arabidopsis thaliana telomerase TERT-TR complex
