ArticleProceedings of the National Academy of Sciences of the United States of America2011
RNA-protein binding interface in the telomerase ribonucleoprotein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 70 citations in OpenAlex.
- Structures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.Nature communications · 2026Article
- A degenerate telomerase RNA directs telomeric DNA synthesis in lepidopteran insects.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular and Evolutionary Analysis of RNA-Protein Interactions in Telomerase Regulation.Non-coding RNA · 2024Review
- RNA as a Major-Groove Ligand: RNA-RNA and RNA-DNA Triplexes Formed by GAA and UUC or TTC Sequences.ACS omega · 2022Article
- Biogenesis of telomerase RNA from a protein-coding mRNA precursor.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural biology of human telomerase: progress and prospects.Biochemical Society transactions · 2021Review
- Arabidopsis retains vertebrate-type telomerase accessory proteins via a plant-specific assembly.Nucleic acids research · 2021Article
- Crystal structures of N-terminally truncated telomerase reverse transcriptase from fungi‡.Nucleic acids research · 2021Article
- Monophyletic Origin and Divergent Evolution of Animal Telomerase RNA.Molecular biology and evolution · 2021Article
- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Folding heterogeneity in the essential human telomerase RNA three-way junction.RNA (New York, N.Y.) · 2020Article
- Dim and Dmoc Protecting Groups for Oligodeoxynucleotide Synthesis.Current protocols in nucleic acid chemistry · 2020Article
- Human Telomerase RNA: Telomerase Component or More?Biomolecules · 2020Review
- Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020Review
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- Quantitative Biology of Human Shelterin and Telomerase: Searching for the Weakest Point.International journal of molecular sciences · 2019Review
- How RNAi machinery enters the world of telomerase.Cell cycle (Georgetown, Tex.) · 2019Review
- Defining the RNA interactome by total RNA-associated protein purification.Molecular systems biology · 2019Article
- Incorporation of Sensitive Ester and Chloropurine Groups into Oligodeoxynucleotides through Solid Phase Synthesis.ChemistrySelect · 2018Article
- Post-transcriptional labeling by using Suzuki-Miyaura cross-coupling generates functional RNA probes.Nucleic acids research · 2018Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Telomerase is a specialized reverse transcriptase containing an intrinsic telomerase RNA (TR) which provides the template for telomeric DNA synthesis. Distinct from conventional reverse transcriptases, telomerase has evolved a unique TR-binding domain (TRBD) in the catalytic telomerase reverse transcriptase (TERT) protein, integral for ribonucleoprotein assembly. Two structural elements in the vertebrate TR, the pseudoknot and CR4/5, bind TERT independently and are essential for telomerase enzymatic activity. However, the details of the TR-TERT interaction have remained elusive. In this study, we employed a photoaffinity cross-linking approach to map the CR4/5-TRBD RNA-protein binding interface by identifying RNA and protein residues in close proximity. Photoreactive 5-iodouridines were incorporated into the medaka CR4/5 RNA fragment and UV cross-linked to the medaka TRBD protein fragment. The cross-linking RNA residues were identified by alkaline partial hydrolysis and cross-linked protein residues were identified by mass spectrometry. Three CR4/5 RNA residues (U182, U187, and U205) were found cross-linking to TRBD amino acids Tyr503, Phe355, and Trp477, respectively. This CR4/5 binding pocket is distinct and separate from the previously proposed T pocket in the Tetrahymena TRBD. Based on homologous structural models, our cross-linking data position the essential loop L6.1 adjacent to the TERT C-terminal extension domain. We thus propose that stem-loop 6.1 facilitates proper TERT folding by interacting with both TRBD and C-terminal extension. Revealing the telomerase CR4/5-TRBD binding interface with single-residue resolution provides important insights into telomerase ribonucleoprotein architecture and the function of the essential CR4/5 domain.
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