ArticleThe Journal of biological chemistry2012
Specificity requirements for human telomere protein interaction with telomerase holoenzyme.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
83 citing papers in PubMed, 112 citations in OpenAlex.
- Biogenesis and Regulation of Telomerase during Development and Cancer.Cold Spring Harbor perspectives in biology · 2026Review
- Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.Science (New York, N.Y.) · 2026Article
- Recent progress in human telomerase structure and its therapeutic targeting.Frontiers in molecular biosciences · 2025Review
- Telomere Reprogramming and Cellular Metabolism: Is There a Link?International journal of molecular sciences · 2024Review
- Structural biology of shelterin and telomeric chromatin: the pieces and an unfinished puzzle.Biochemical Society transactions · 2024Review
- Telomere C-Strand Fill-In Machinery: New Insights into the Human CST-DNA Polymerase Alpha-Primase Structures and Functions.Sub-cellular biochemistry · 2024Review
- Models for human telomere C-strand fill-in by CST-Polα-primase.Trends in biochemical sciences · 2023Review
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Telomerase structural biology comes of age.Current opinion in structural biology · 2022Review
- Proteomic Identification of Potential Target Proteins of Cathepsin W for Its Development as a Drug Target for Influenza.Microbiology spectrum · 2022Article
- Article
- Structural basis of human telomerase recruitment by TPP1-POT1.Science (New York, N.Y.) · 2022Article
- Differential impact of a dyskeratosis congenita mutation in TPP1 on mouse hematopoiesis and germline.Life science alliance · 2022Article
- Structural biology of human telomerase: progress and prospects.Biochemical Society transactions · 2021Review
- The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- TPP1 mutagenesis screens unravel shelterin interfaces and functions in hematopoiesis.JCI insight · 2021Article
- Article
- Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization.Nature reviews. Molecular cell biology · 2021Review
- Identification and characterization of novelCold Spring Harbor molecular case studies · 2021Article
- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
23 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Human telomeres are maintained by the enzyme telomerase, which uses a template within its integral RNA subunit (hTR) and telomerase reverse transcriptase protein (TERT) to accomplish the synthesis of single-stranded DNA repeats. Many questions remain unresolved about the cellular regulation of telomerase subunits and the fully assembled telomerase holoenzyme, including the basis for the specificity of binding and acting on telomeres. Previous studies have revealed that the telomere protein TPP1 is necessary for stable TERT and hTR association with telomeres in vivo. Here, we expand the biochemical characterization and understanding of TPP1 interaction with TERT and the catalytically active telomerase holoenzyme. Using extracts from human cells, we show that TPP1 interacts sequence-specifically with TERT when TERT is assembled into holoenzyme context. In holoenzyme context, the TERT N-terminal domain mediates a TPP1 interaction. Assays of stable subunit complexes purified after their cellular assembly suggest that other telomere proteins do not necessarily influence TPP1 association with telomerase holoenzyme or alter its impact on elongation processivity. We show that a domain of recombinant TPP1 comprised of an oligonucleotide/oligosaccharide binding fold recapitulates the full-length protein interaction specificity for the TERT N-terminal domain assembled into telomerase holoenzyme. By global analysis of TPP1 side chain requirements for holoenzyme association, we demonstrate a selective requirement for the amino acids in one surface-exposed protein loop. Our results reveal the biochemical determinants of a sequence-specific TPP1-TERT interaction in human cells, with implications for the mechanisms of TPP1 function in recruiting telomerase subunits to telomeres and in promoting telomere elongation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.