Evidence map›Paper›PMID 9585510›Full record

ArticleGenes & development1998

Modulation of telomerase activity by telomere DNA-binding proteins in Oxytricha.

S J Froelich-Ammon, B A Dickinson, J M Bevilacqua, S C Schultz, T R Cech

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Review
  3. Multiple facets of TPP1 in telomere maintenance.Biochimica et biophysica acta · 2014
    Review
  4. Article
  5. Article
  6. Review
  7. Pot1 and telomere maintenance.FEBS letters · 2010
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Human POT1 disrupts telomeric G-quadruplexes allowing telomerase extension in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Nucleic acid recognition by OB-fold proteins.Annual review of biophysics and biomolecular structure · 2003
    Review
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 2 institutions in 1 country.

S J Froelich-AmmonDepartment of Chemistry and Biochemistry and Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado 80309-0215, USA. thomas.cech@colorado.edu
B A Dickinson
J M Bevilacqua
S C Schultz
T R Cech
University of Colorado Boulder · USHoward Hughes Medical Institute · US

Funding

Telomerase and Telomeres: Structure, Function/RegulationR01GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS ROBERT · 1985 to 2009
$2.6M
CRYSTAL STRUCTURE OF A TELOMERIC PROTEIN-DNA COMPLEXF32GM017155 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI BEVILACQUA, JOANNE M · 1994 to 1995
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THREE-DIMENSIONAL STRUCTURE OF THE ENDS OF CHROMOSOMESR01AG011636 · NIA · UNIVERSITY OF COLORADO AT BOULDER · PI SCHULTZ, STEVE C · 1993 to 1997
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STUDIES OF NUCLEIC ACID STRUCTURE AND REACTIVITYR37GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS R · 1988 to 1997
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NIA NIH HHS AG11636NIGMS NIH HHS F32 GM017155NIGMS NIH HHS GM17155NIGMS NIH HHS GM28039NIGMS NIH HHS R01 GM028039
6 · The paper itself

Abstract

Telomere proteins protect the chromosomal terminus from nucleolytic degradation and end-to-end fusion, and they may contribute to telomere length control and the regulation of telomerase. The current studies investigate the effect of Oxytricha single-stranded telomere DNA-binding protein subunits alpha and beta on telomerase elongation of telomeric DNA. A native agarose gel system was used to evaluate telomere DNA-binding protein complex composition, and the ability of telomerase to use these complexes as substrates was characterized. Efficient elongation occurred in the presence of the alpha subunit. Moreover, the alpha-DNA cross-linked complex was a substrate for telomerase. At higher alpha concentrations, two alpha subunits bound to the 16-nucleotide single-stranded DNA substrate and rendered it inaccessible to telomerase. The formation of this alpha . DNA . alpha complex may contribute to regulation of telomere length. The alpha . beta . DNA ternary complex was not a substrate for telomerase. Even when telomerase was prebound to telomeric DNA, the addition of alpha and beta inhibited elongation, suggesting that these telomere protein subunits have a greater affinity for the DNA and are able to displace telomerase. In addition, the ternary complex was not a substrate for terminal deoxynucleotidyltransferase. We conclude that the telomere protein inhibits telomerase by rendering the telomeric DNA inaccessible, thereby helping to maintain telomere length.

Indexed as

AnimalsDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA NucleotidylexotransferaseDNA, ProtozoanDNA, Single-StrandedElectrophoresis, Agar GelMacromolecular SubstancesModels, GeneticOxytrichaProtein BindingProtozoan ProteinsRepetitive Sequences, Nucleic AcidSpecies SpecificityTelomeraseTelomereDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA NucleotidylexotransferaseDNA, ProtozoanDNA, Single-StrandedMacromolecular SubstancesProtozoan ProteinsTelomerase

Identifiers

PMID9585510
PMCPMC316840
OpenAlexW2028618193

What OpenQuestion holds

Textmetadata
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.