Evidence map›Paper›PMID 37624885›Full record

ArticleScience advances2023

Structural basis of telomeric nucleosome recognition by shelterin factor TRF1.

Hongmiao Hu, Anne-Marie M van Roon, George E Ghanim, Bilal Ahsan, Abraham O Oluwole, Sew-Yeu Peak-Chew, Carol V Robinson, Thi Hoang Duong Nguyen

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. TRF1 and TRF2: pioneering targets in telomere-based cancer therapy.Journal of cancer research and clinical oncology · 2024
    Review
  8. Review
  9. 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

8 authors at 2 institutions in 1 country.

Hongmiao HuMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.ORCID 0000-0002-3086-3072
Anne-Marie M van RoonMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.ORCID 0000-0002-4435-9926
George E GhanimMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.ORCID 0000-0002-3341-3122
Bilal AhsanMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.ORCID 0000-0003-1839-5023
Abraham O OluwoleDepartment of Chemistry, University of Oxford, Oxford, OX1 3QZ UK.ORCID 0000-0001-8647-4781
Sew-Yeu Peak-ChewMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.
Carol V RobinsonDepartment of Chemistry, University of Oxford, Oxford, OX1 3QZ UK.ORCID 0000-0001-7829-5505
Thi Hoang Duong NguyenMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.ORCID 0000-0002-2180-3430
MRC Laboratory of Molecular Biology · GBUniversity of Oxford · GB

Funding

Medical Research Council MC_UP_1201/19Medical Research Council MR/V028839/1
6 · The paper itself

Abstract

Shelterin and nucleosomes are the key players that organize mammalian chromosome ends into the protective telomere caps. However, how they interact with each other at telomeres remains unknown. We report cryo-electron microscopy structures of a human telomeric nucleosome both unbound and bound to the shelterin factor TRF1. Our structures reveal that TRF1 binds unwrapped nucleosomal DNA ends by engaging both the nucleosomal DNA and the histone octamer. Unexpectedly, TRF1 binding shifts the register of the nucleosomal DNA by 1 bp. We discovered that phosphorylation of the TRF1 C terminus and a noncanomical DNA binding surface on TRF1 are critical for its association with telomeric nucleosomes. These insights into shelterin-chromatin interactions have crucial implications for understanding telomeric chromatin organization and other roles of shelterin at telomeres including replication and transcription.

Indexed as

NucleosomesTelomereAnimalsChromatinChromosomes, MammalianCryoelectron MicroscopyHumansMammalsTelomeric Repeat Binding Protein 1ChromatinNucleosomesTelomeric Repeat Binding Protein 1

Identifiers

PMID37624885
PMCPMC10456876
OpenAlexW4386156797

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.