ArticleMolecular biology of the cell2003
Tetrahymena telomerase is active as a monomer.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 47 citations in OpenAlex.
- In vivo architecture of the telomerase RNA catalytic core in Trypanosoma brucei.Nucleic acids research · 2021Article
- Structural accommodations accompanying splicing of a group II intron RNP.Nucleic acids research · 2018Article
- Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017Review
- Progress in Human and Tetrahymena Telomerase Structure Determination.Annual review of biophysics · 2017Review
- Current Insights to Regulation and Role of Telomerase in Human Diseases.Antioxidants (Basel, Switzerland) · 2017Review
- Structure of a group II intron in complex with its reverse transcriptase.Nature structural & molecular biology · 2016Article
- Article
- Article
- The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids.Nucleic acids research · 2015Article
- Human telomerase: biogenesis, trafficking, recruitment, and activation.Genes & development · 2015Review
- Telomerase structure.Current opinion in structural biology · 2014Review
- Progress in structural studies of telomerase.Current opinion in structural biology · 2014Review
- Functional importance of telomerase pseudoknot revealed by single-molecule analysis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Ribonucleoprotein multimers and their functions.Critical reviews in biochemistry and molecular biology · 2010Review
- A single-molecule assay for telomerase structure-function analysis.Nucleic acids research · 2010Article
- Disease-associated human telomerase RNA variants show loss of function for telomere synthesis without dominant-negative interference.Molecular and cellular biology · 2008Article
- Multiple DNA-binding sites in Tetrahymena telomerase.Nucleic acids research · 2008Article
- Structural analysis of the catalytic core of human telomerase RNA by FRET and molecular modeling.Biochemistry · 2006Article
- Structure of stem-loop IV of Tetrahymena telomerase RNA.The EMBO journal · 2006Article
- The biogenesis and regulation of telomerase holoenzymes.Nature reviews. Molecular cell biology · 2006Review
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 2 institutions in 2 countries.
Funding
Abstract
Telomerase is an enzyme that utilizes an internal RNA molecule as a template for the extension of chromosomal DNA ends. The catalytic core of telomerase consists of the RNA subunit and a protein reverse transcriptase subunit, known as telomerase reverse transcriptase (TERT). It has previously been shown that both yeast and human telomerase can form dimers or multimers in which one RNA in the complex can influence the activity of another. To test the proposal that dimerization might be essential for telomerase activity, we sought to determine whether Tetrahymena thermophila telomerase is active as a dimer or a monomer. Recombinant Tetrahymena telomerase eluted from a gel filtration column at the size of a monomeric complex (one RNA plus one TERT), and those fractions showed processive telomerase activity. We were unable to detect dimerization of Tetrahymena telomerase by coprecipitation experiments, by using tags on either the TERT protein or telomerase RNA. Therefore, a majority, if not all, of the recombinant Tetrahymena telomerase in our reconstitution system is present as a monomeric complex. We were also unable to detect dimerization of native telomerase from mating and vegetative Tetrahymena cell extracts. These results demonstrate that Tetrahymena telomerase does not need to dimerize to be active and processive.
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.