Evidence map›Paper›PMID 22981946›Full record

ArticleStructure (London, England : 1993)2012

POT1-TPP1 regulates telomeric overhang structural dynamics.

Helen Hwang, Noah Buncher, Patricia L Opresko, Sua Myong

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

86 citing papers in PubMed, 133 citations in OpenAlex.

  1. Review
  2. Protection of the Telomeric Junction by the Shelterin Complex.Journal of the American Chemical Society · 2024
    Article
  3. Protection of the Telomeric Junction by the Shelterin Complex.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Telomere maintenance in African trypanosomes.Frontiers in molecular biosciences · 2023
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Creation and resolution of non-B-DNA structural impediments during replication.Critical reviews in biochemistry and molecular biology · 2022
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

26 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Helen HwangBioengineering Department, University of Illinois, Urbana, IL 61801, USA.
Noah Buncher
Patricia L Opresko
Sua Myong
University of Illinois Urbana-Champaign · USUniversity of Pittsburgh · US

Funding

Quantitative Stepwise Analysis of RNA InterferenceDP2GM105453 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MYONG, SUA · 2012 to 2012
$2.4M
Mechanisms of Telomeric DNA Loss and RepairR01ES015052 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI OPRESKO, PATRICIA L · 2006 to 2010
$2.4M
The Role of Structural Dynamics on Telomeric End AccessibilityF30CA174323 · NCI · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI HWANG, HELEN · 2013 to 2015
$135k
NCI NIH HHS F30 CA174323NIEHS NIH HHS ES0515052NIEHS NIH HHS R01 ES015052NIGMS NIH HHS DP2 GM105453
6 · The paper itself

Abstract

Human telomeres possess a single-stranded DNA (ssDNA) overhang of TTAGGG repeats, which can self-fold into a G-quadruplex structure. POT1 binds specifically to the telomeric overhang and partners with TPP1 to regulate telomere lengthening and capping, although the mechanism remains elusive. Here, we show that POT1 binds stably to folded telomeric G-quadruplex DNA in a sequential manner, one oligonucleotide/oligosaccharide binding fold at a time. POT1 binds from 3' to 5', thereby unfolding the G-quadruplex in a stepwise manner. In contrast, the POT1-TPP1 complex induces a continuous folding and unfolding of the G-quadruplex. We demonstrate that POT1-TPP1 slides back and forth on telomeric DNA and also on a mutant telomeric DNA to which POT1 cannot bind alone. The sliding motion is specific to POT1-TPP1, as POT1 and ssDNA binding protein gp32 cannot recapitulate this activity. Our results reveal fundamental molecular steps and dynamics involved in telomere structure regulation.

Indexed as

TelomereDNA PrimersHumansProtein ConformationProtein FoldingShelterin ComplexTelomere-Binding ProteinsACD protein, humanDNA PrimersPOT1 protein, humanShelterin ComplexTelomere-Binding Proteins

Identifiers

PMID22981946
PMCPMC4109716
OpenAlexW2135003636

What OpenQuestion holds

Textmetadata
LicenceTDM
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.