ArticleCell research2021
Zipper head mechanism of telomere synthesis by human telomerase.
Article in Cell research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 42 citations in OpenAlex.
- Structures of human telomerase with BIBR1532 reveal novel mechanism of inhibition.Nature chemical biology · 2026Article
- Biogenesis and Regulation of Telomerase during Development and Cancer.Cold Spring Harbor perspectives in biology · 2026Review
- Article
- Extreme Kinetic Stability and RNase Resistance of Human Telomerase RNA G-Quadruplexes Overcome by DHX36 Helicase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.Nature communications · 2026Article
- Decoding RNA triple helices: identification from sequence and secondary structure.Briefings in bioinformatics · 2026Article
- Article
- Cryo-EM structure of human telomerase dimer reveals H/ACA RNP-mediated dimerization.Science (New York, N.Y.) · 2025Article
- A (Scientific) Lifetime Affair With Nucleic Acids.Journal of molecular biology · 2025Review
- H/ACA snR30 snoRNP guides independent 18S rRNA subdomain formation.Nature communications · 2025Article
- A Modular Engineered DNA Nanodevice for Precise Profiling of Telomerase RNA Location and Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.Nature communications · 2025Article
- Recent progress in human telomerase structure and its therapeutic targeting.Frontiers in molecular biosciences · 2025Review
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.bioRxiv : the preprint server for biology · 2024Article
- A persistent variant telomere sequence in a human pedigree.Nature communications · 2024Article
- The SUN-family protein Sad1 mediates heterochromatin spatial organization through interaction with histone H2A-H2B.Nature communications · 2024Article
- Characterisation of the Arabidopsis thaliana telomerase TERT-TR complex.Plant molecular biology · 2024Article
- Methods that shaped telomerase research.Biogerontology · 2024Review
- 2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein.Nature communications · 2024Article
- Telomere C-Strand Fill-In Machinery: New Insights into the Human CST-DNA Polymerase Alpha-Primase Structures and Functions.Sub-cellular biochemistry · 2024Review
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Telomerase, a multi-subunit ribonucleoprotein complex, is a unique reverse transcriptase that catalyzes the processive addition of a repeat sequence to extend the telomere end using a short fragment of its own RNA component as the template. Despite recent structural characterizations of human and Tetrahymena telomerase, it is still a mystery how telomerase repeatedly uses its RNA template to synthesize telomeric DNA. Here, we report the cryo-EM structure of human telomerase holoenzyme bound with telomeric DNA at resolutions of 3.5 Å and 3.9 Å for the catalytic core and biogenesis module, respectively. The structure reveals that a leucine residue Leu980 in telomerase reverse transcriptase (TERT) catalytic subunit functions as a zipper head to limit the length of the short primer-template duplex in the active center. Moreover, our structural and computational analyses suggest that TERT and telomerase RNA (hTR) are organized to harbor a preformed active site that can accommodate short primer-template duplex substrates for catalysis. Furthermore, our findings unveil a double-fingers architecture in TERT that ensures nucleotide addition processivity of human telomerase. We propose that the zipper head Leu980 is a structural determinant for the sequence-based pausing signal of DNA synthesis that coincides with the RNA element-based physical template boundary. Functional analyses unveil that the non-glycine zipper head plays an essential role in both telomerase repeat addition processivity and telomere length homeostasis. In addition, we also demonstrate that this zipper head mechanism is conserved in all eukaryotic telomerases. Together, our study provides an integrated model for telomerase-mediated telomere synthesis.
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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.