Evidence map›Paper›PMID 14681592›Full record

ArticleRNA (New York, N.Y.)2004

Analysis of a long-range interaction between conserved domains of human telomerase RNA.

Christine T Ueda, Richard W Roberts

Abstract readComparative Study
In one paragraph

Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Review
  2. Telomerase RNA stem terminus element affects template boundary element function, telomere sequence, and shelterin binding.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  3. Telomere les(i/s)ons from a telomerase RNA mutant.Cell cycle (Georgetown, Tex.) · 2015
    Review
  4. Article
  5. Article
  6. RNA-protein binding interface in the telomerase ribonucleoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  7. Architecture of human telomerase RNA.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  8. Telomerase: an RNP enzyme synthesizes DNA.Cold Spring Harbor perspectives in biology · 2011
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Christine T UedaDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Richard W Roberts

Funding

IN VITRO SELECTION OF PROTEINS VIA MRNA-PROTEIN FUSIONSR01GM060416 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI ROBERTS, RICHARD W · 2000 to 2010
$2.9M
NIGMS NIH HHS R01 GM060416NIGMS NIH HHS R01 GM60416
6 · The paper itself

Abstract

Telomerase is a ribonucleoprotein complex responsible for maintaining telomere length of eukaryotic chromosomes. Human telomerase has two main components, the human telomerase reverse transcriptase and the human telomerase RNA (hTR). Two domains of hTR essential for telomerase activity are the template domain, comprised of an 11-nt templating and alignment sequence, and the CR4/CR5 domain. Highly conserved residues in the CR4/CR5 domain form the stem-loop P6.1, which is important for assembly and activity of mammalian telomerase. Here, we have determined that stem-loop P6.1 can participate in a long-range RNA-RNA interaction with the template region of hTR. We characterized this interaction through mobility shift assays, mutation analysis, and UV cross-linking experiments. Mutation analysis revealed that the P6.1 loop nucleotides participate in the interaction with the template. The site of interaction at the template domain was determined via UV cross-linking experiments. These data show that an RNA-RNA interaction exists between two highly conserved regions of hTR that are critical for the higher order folding of telomerase RNA. This interaction argues for the proximity of the template and the CR4/CR5 domain, and provides the basis for a revised model of hTR, partitioning the RNA into a catalytic domain and a localization domain.

Indexed as

Base PairingBase SequenceBinding SitesCatalytic DomainCross-Linking ReagentsDNA-Binding ProteinsElectrophoretic Mobility Shift AssayHumansMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingRNATelomeraseTemplates, GeneticUltraviolet RaysCross-Linking ReagentsDNA-Binding ProteinsRNATelomerasetelomerase RNA

Identifiers

PMID14681592
PMCPMC1370525

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.