ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structurally conserved five nucleotide bulge determines the overall topology of the core domain of human telomerase RNA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 65 citations in OpenAlex.
- Structure guided discovery of small molecule ligands targeting the oncomiR-1 NPSL2 hairpin.Scientific reports · 2025Article
- A (Scientific) Lifetime Affair With Nucleic Acids.Journal of molecular biology · 2025Review
- Conformational plasticity and allosteric communication networks explain Shelterin protein TPP1 binding to human telomerase.Communications chemistry · 2023Article
- Telomerase structural biology comes of age.Current opinion in structural biology · 2022Review
- How Structural Features Define Biogenesis and Function of Human Telomerase RNA Primary Transcript.Biomedicines · 2022Review
- Pharmacophore-Based Discovery of Viral RNA Conformational Modulators.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Article
- Evolutionary conservation of RNA sequence and structure.Wiley interdisciplinary reviews. RNA · 2021Review
- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Rapid and accurate determination of atomistic RNA dynamic ensemble models using NMR and structure prediction.Nature communications · 2020Article
- Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy.Molecules (Basel, Switzerland) · 2020Review
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018Review
- Current Perspectives of Telomerase Structure and Function in Eukaryotes with Emerging Views on Telomerase in Human Parasites.International journal of molecular sciences · 2018Review
- Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017Review
- An excited state underlies gene regulation of a transcriptional riboswitch.Nature chemical biology · 2017Article
- Progress in Human and Tetrahymena Telomerase Structure Determination.Annual review of biophysics · 2017Review
- Determination of the conformational ensemble of the TAR RNA by X-ray scattering interferometry.Nucleic acids research · 2017Article
- How do ADARs bind RNA? New protein-RNA structures illuminate substrate recognition by the RNA editing ADARs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- Single-molecule FRET-Rosetta reveals RNA structural rearrangements during human telomerase catalysis.RNA (New York, N.Y.) · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Telomerase is a unique ribonucleoprotein complex that catalyzes the addition of telomeric DNA repeats onto the 3' ends of linear chromosomes. All vertebrate telomerase RNAs contain a catalytically essential core domain that includes the template and a pseudoknot with extended helical subdomains. Within these helical regions is an asymmetric 5-nt internal bulge loop (J2a/b) flanked by helices (P2a and P2b) that is highly conserved in its location but not sequence. NMR structure determination reveals that J2a/b forms a defined S-shape and creates an ∼90 ° bend with a surprisingly low twist (∼10 °) between the flanking helices. A search of RNA structures revealed only one other example of a 5-nt bulge, from hepatitis C virus internal ribosome entry site, with a different sequence but the same structure. J2a/b is intrinsically flexible but the interhelical motions across the loop are remarkably restricted. Nucleotide substitutions in J2a/b that affect the bend angle, direction, and interhelical dynamics are correlated with telomerase activity. Based on the structures of P2ab (J2a/b and flanking helices), the conserved region of the pseudoknot (P2b/P3, previously determined) and the remaining helical segment (P2a.1-J2a.1 refined using residual dipolar couplings and the modeling program MC-Sym) we have calculated an NMR-based model of the full-length pseudoknot. The model and dynamics analysis show that J2a/b serves as a dominant structural and dynamical element in defining the overall topology of the core domain, and suggest that interhelical motions in P2ab facilitate nucleotide addition along the template and template translocation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.