Evidence map›Paper›PMID 26457608›Full record

ArticleeLife2015

Single-molecule imaging of telomerase reverse transcriptase in human telomerase holoenzyme and minimal RNP complexes.

Robert Alexander Wu, Yavuz S Dagdas, S Tunc Yilmaz, Ahmet Yildiz, Kathleen Collins

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. 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
3.4field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Single-Run Catalysis and Kinetic Control of Human Telomerase Holoenzyme.Advances in experimental medicine and biology · 2022
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017
    Review
  17. Article
  18. Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017
    Review
  19. Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017
    Review
  20. 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 1 institution in 1 country.

Robert Alexander WuDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Yavuz S DagdasBiophysics Graduate Group, University of California, Berkeley, Berkeley, United States.
S Tunc YilmazDepartment of Physics, University of California, Berkeley, Berkeley, United States.
Ahmet YildizDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Kathleen CollinsDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
University of California, Berkeley · US

Funding

STRUCTURE AND FUNCTION OF TELOMERASER01GM054198 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 1996 to 2018
$5.4M
Molecular Mechanism of X-linked Dyskeratosis CongenitaR01HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2004 to 2017
$4.1M
Understanding the Mechanism and Regulation of the Human Cytoplasmic Dynein ComplexR01GM094522 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI YILDIZ, AHMET · 2011 to 2019
$2.8M
Structural and Functional Characterization of Telomere Protection and MaintenanceR01GM118773 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI YILDIZ, AHMET · 2016 to 2019
$1.2M
Biogenesis and Regulation of Human TelomeraseR56HL079585 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 2008 to 2008
$367k
NHLBI NIH HHS HL079585NIGMS NIH HHS GM054198NIGMS NIH HHS GM094522NIGMS NIH HHS R01 GM054198NIGMS NIH HHS R01 GM094522NIGMS NIH HHS R01 GM118773
6 · The paper itself

Abstract

Telomerase synthesizes chromosome-capping telomeric repeats using an active site in telomerase reverse transcriptase (TERT) and an integral RNA subunit template. The fundamental question of whether human telomerase catalytic activity requires cooperation across two TERT subunits remains under debate. In this study, we describe new approaches of subunit labeling for single-molecule imaging, applied to determine the TERT content of complexes assembled in cells or cell extract. Surprisingly, telomerase reconstitutions yielded heterogeneous DNA-bound TERT monomer and dimer complexes in relative amounts that varied with assembly and purification method. Among the complexes, cellular holoenzyme and minimal recombinant enzyme monomeric for TERT had catalytic activity. Dimerization was suppressed by removing a TERT domain linker with atypical sequence bias, which did not inhibit cellular or minimal enzyme assembly or activity. Overall, this work defines human telomerase DNA binding and synthesis properties at single-molecule level and establishes conserved telomerase subunit architecture from single-celled organisms to humans.

Indexed as

Cell LineHumansModels, BiologicalModels, ChemicalOptical ImagingProtein MultimerizationTelomeraseTelomereTelomerasebiophysicschromosomesfluorescence imaginggeneshumanstructural biologytelomerasetelomeric repeat synthesis

Identifiers

PMID26457608
PMCPMC4600948
OpenAlexW2194942599

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.