Evidence map›Paper›PMID 20044353›Full record

ArticleNucleic acids research2010

A novel motif in telomerase reverse transcriptase regulates telomere repeat addition rate and processivity.

Mingyi Xie, Joshua D Podlevsky, Xiaodong Qi, Christopher J Bley, Julian J-L Chen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
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

49 citing papers in PubMed, 72 citations in OpenAlex.

  1. Telomerase mutations in smokers with severe emphysema.The Journal of clinical investigation · 2015
    Trial
  2. Article
  3. Article
  4. Article
  5. A degenerate telomerase RNA directs telomeric DNA synthesis in lepidopteran insects.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Telomerase structural biology comes of age.Current opinion in structural biology · 2022
    Review
  11. Article
  12. Flexibility of telomerase in binding the RNA template and DNA telomeric repeat.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Origin and Fates ofInternational journal of molecular sciences · 2021
    Article
  15. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Review
  17. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Mingyi XieDepartment of Chemistry & Biochemistry and School of Life Sciences, Arizona State University, Tempe, AZ 85287-1604, USA.
Joshua D Podlevsky
Xiaodong Qi
Christopher J Bley
Julian J-L Chen
Arizona State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Telomerase is a specialized reverse transcriptase that adds telomeric DNA repeats onto chromosome termini. Here, we characterize a new telomerase-specific motif, called motif 3, in the catalytic domain of telomerase reverse transcriptase, that is crucial for telomerase function and evolutionally conserved between vertebrates and ciliates. Comprehensive mutagenesis of motif 3 identified mutations that remarkably increase the rate or alter the processivity of telomere repeat addition. Notably, the rate and processivity of repeat addition are affected independently by separate motif 3 mutations. The processive telomerase action relies upon a template translocation mechanism whereby the RNA template and the telomeric DNA strand separate and realign between each repeat synthesis. By analyzing the mutant telomerases reconstituted in vitro and in cells, we show that the hyperactive mutants exhibit higher repeat addition rates and faster enzyme turnovers, suggesting higher rates of strand-separation during template translocation. In addition, the strong correlation between the processivity of the motif 3 mutants and their ability to use an 8 nt DNA primer, suggests that motif 3 facilitates realignment between the telomeric DNA and the template RNA following strand-separation. These findings support motif 3 as a key determinant for telomerase activity and processivity.

Indexed as

Amino Acid MotifsAmino Acid SequenceConserved SequenceDNA PrimersHumansModels, MolecularMolecular Sequence DataMutationRepetitive Sequences, Nucleic AcidSequence Homology, Amino AcidTelomeraseTelomereDNA PrimersTelomeraseTERT protein, human

Identifiers

PMID20044353
PMCPMC2847249
OpenAlexW1990625302

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.