ArticleRNA (New York, N.Y.)2020
Folding heterogeneity in the essential human telomerase RNA three-way junction.
Article in RNA (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- The Unpaved Road of Non-Coding RNA Structure-Function Relationships: Current Knowledge, Available Methodologies, and Future Trends.Non-coding RNA · 2025Review
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.Nature communications · 2025Article
- A systematic search for RNA structural switches across the human transcriptome.Nature methods · 2024Article
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.bioRxiv : the preprint server for biology · 2024Article
- Massively parallel dissection of RNA in RNA-protein interactions in vivo.Nucleic acids research · 2024Article
- Advances in understanding telomerase assembly.Biochemical Society transactions · 2023Review
- RNA:RNA interaction in ternary complexes resolved by chemical probing.RNA (New York, N.Y.) · 2023Article
- Article
- 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
- Article
- Article
- U2 snRNA structure is influenced by SF3A and SF3B proteins but not by SF3B inhibitors.PloS one · 2021Article
- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Anomalous Reverse Transcription through Chemical Modifications in Polyadenosine Stretches.Biochemistry · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Telomeres safeguard the genome by suppressing illicit DNA damage responses at chromosome termini. To compensate for incomplete DNA replication at telomeres, most continually dividing cells, including many cancers, express the telomerase ribonucleoprotein (RNP) complex. Telomerase maintains telomere length by catalyzing de novo synthesis of short DNA repeats using an internal telomerase RNA (TR) template. TRs from diverse species harbor structurally conserved domains that contribute to RNP biogenesis and function. In vertebrate TRs, the conserved regions 4 and 5 (CR4/5) fold into a three-way junction (TWJ) that binds directly to the telomerase catalytic protein subunit and is required for telomerase function. We have analyzed the structural properties of the human TR (hTR) CR4/5 domain using a combination of in vitro chemical mapping, secondary structural modeling, and single-molecule structural analysis. Our data suggest the essential P6.1 stem-loop within CR4/5 is not stably folded in the absence of the telomerase reverse transcriptase in vitro. Rather, the hTR CR4/5 domain adopts a heterogeneous ensemble of conformations. Finally, single-molecule FRET measurements of CR4/5 and a mutant designed to stabilize the P6.1 stem demonstrate that TERT binding selects for a structural conformation of CR4/5 that is not the dominant state of the TERT-free in vitro RNA ensemble.
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