Evidence map›Paper›PMID 22315458›Full record

ArticleRNA (New York, N.Y.)2012

The C-terminal domain of Tetrahymena thermophila telomerase holoenzyme protein p65 induces multiple structural changes in telomerase RNA.

Benjamin M Akiyama, John Loper, Kevin Najarro, Michael D Stone

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Telomerase structural biology comes of age.Current opinion in structural biology · 2022
    Review
  4. Article
  5. Structure ofRNA biology · 2021
    Article
  6. Review
  7. Article
  8. Review
  9. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  10. Article
  11. Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Progress in structural studies of telomerase.Current opinion in structural biology · 2014
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  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

4 authors at 1 institution in 2 countries.

Benjamin M AkiyamaDepartment of Molecular, Cell, and Developmental Biology, University of California, Santa Cruz, Santa Cruz, California 95064, USA.
John Loper
Kevin Najarro
Michael D Stone
University of California, Santa Cruz · US

Funding

Structure and dynamics of the Tetrahymena telomerase ribonucleoproteinR01GM095850 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STONE, MICHAEL D · 2011 to 2023
$4.4M
Training Program/Molecular/Cell/Developmental BiologyT32GM008646 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STROME, SUSAN · 1999 to 2018
$3.7M
NIGMS NIH HHS GM095850NIGMS NIH HHS R01 GM095850NIGMS NIH HHS T32 GM008646NIGMS NIH HHS T32 GM8646
6 · The paper itself

Abstract

The unique cellular activity of the telomerase reverse transcriptase ribonucleoprotein (RNP) requires proper assembly of protein and RNA components into a functional complex. In the ciliate model organism Tetrahymena thermophila, the La-domain protein p65 is required for in vivo assembly of telomerase. Single-molecule and biochemical studies have shown that p65 promotes efficient RNA assembly with the telomerase reverse transcriptase (TERT) protein, in part by inducing a bend in the conserved stem IV region of telomerase RNA (TER). The domain architecture of p65 consists of an N-terminal domain, a La-RRM motif, and a C-terminal domain (CTD). Using single-molecule Förster resonance energy transfer (smFRET), we demonstrate the p65(CTD) is necessary for the RNA remodeling activity of the protein and is sufficient to induce a substantial conformational change in stem IV of TER. Moreover, nuclease protection assays directly map the site of p65(CTD) interaction to stem IV and reveal that, in addition to bending stem IV, p65 binding reorganizes nucleotides that comprise the low-affinity TERT binding site within stem-loop IV.

Indexed as

Electrophoretic Mobility Shift AssayFluorescence Resonance Energy TransferNucleic Acid ConformationRNATelomeraseTetrahymena thermophilaRNATelomerase

Identifiers

PMID22315458
PMCPMC3312553
OpenAlexW2103694365

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.