ArticleRNA (New York, N.Y.)2017
Single-molecule FRET-Rosetta reveals RNA structural rearrangements during human telomerase catalysis.
Article in RNA (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- FRET-guided selection of RNA 3D structures.Nucleic acids research · 2026Article
- A DNA Scaffold Approach Facilitates 5' Labeling of the SARS-CoV-2 RNA Pseudoknot for Single-Molecule Förster Resonance Energy Transfer Investigation.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- FRET-guided modeling of nucleic acids.Nucleic acids research · 2024Article
- In vivo architecture of the telomerase RNA catalytic core in Trypanosoma brucei.Nucleic acids research · 2021Article
- Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules.Micromachines · 2021Review
- Integrating single-molecule FRET and biomolecular simulations to study diverse interactions between nucleic acids and proteins.Essays in biochemistry · 2021Review
- Structure of membrane diacylglycerol kinase in lipid bilayers.Communications biology · 2021Article
- Automated AFM analysis of DNA bending reveals initial lesion sensing strategies of DNA glycosylases.Scientific reports · 2020Article
- Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy.Molecules (Basel, Switzerland) · 2020Review
- Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019Review
- Programming Structured DNA Assemblies to Probe Biophysical Processes.Annual review of biophysics · 2019Review
- Sampling Native-like Structures of RNA-Protein Complexes through Rosetta Folding and Docking.Structure (London, England : 1993) · 2019Article
- Mechanisms of template handling and pseudoknot folding in human telomerase and their manipulation to expand the sequence repertoire of processive repeat synthesis.Nucleic acids research · 2018Article
- Life under the Microscope: Single-Molecule Fluorescence Highlights the RNA World.Chemical reviews · 2018Review
- A single nucleotide incorporation step limits human telomerase repeat addition activity.The EMBO journal · 2018Article
- New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018Review
- Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017Review
- DNA-binding determinants and cellular thresholds for human telomerase repeat addition processivity.The EMBO journal · 2017Article
- Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017Review
- Fundamental mechanisms of telomerase action in yeasts and mammals: understanding telomeres and telomerase in cancer cells.Open biology · 2017Review
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Authors and funding
4 authors.
Funding
Abstract
Maintenance of telomeres by telomerase permits continuous proliferation of rapidly dividing cells, including the majority of human cancers. Despite its direct biomedical significance, the architecture of the human telomerase complex remains unknown. Generating homogeneous telomerase samples has presented a significant barrier to developing improved structural models. Here we pair single-molecule Förster resonance energy transfer (smFRET) measurements with Rosetta modeling to map the conformations of the essential telomerase RNA core domain within the active ribonucleoprotein. FRET-guided modeling places the essential pseudoknot fold distal to the active site on a protein surface comprising the C-terminal element, a domain that shares structural homology with canonical polymerase thumb domains. An independently solved medium-resolution structure of Tetrahymena telomerase provides a blind test of our modeling methodology and sheds light on the structural homology of this domain across diverse organisms. Our smFRET-Rosetta models reveal nanometer-scale rearrangements within the RNA core domain during catalysis. Taken together, our FRET data and pseudoatomic molecular models permit us to propose a possible mechanism for how RNA core domain rearrangement is coupled to template hybrid elongation.
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