Evidence map›Paper›PMID 26304540›Full record

ArticleNucleic acids research2015

Histone variant H3.3 provides the heterochromatic H3 lysine 9 tri-methylation mark at telomeres.

Maheshi Udugama, Fiona T M Chang, F Lyn Chan, Michelle C Tang, Hilda A Pickett, James D R McGhie, Lynne Mayne, Philippe Collas, Jeffrey R Mann, Lee H Wong

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

74 citing papers in PubMed, 104 citations in OpenAlex.

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  16. Lysine-36 ofbioRxiv : the preprint server for biology · 2023
    Article
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14 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

10 authors at 4 institutions in 2 countries.

Maheshi UdugamaDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Fiona T M ChangDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
F Lyn ChanDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Michelle C TangDepartment of Zoology, University of Melbourne, Parkville, Victoria 3052, Australia.
Hilda A PickettTelomere Length Regulation Group, Children's Medical Research Institute, University of Sydney, Westmead, New South Wales, Australia.
James D R McGhieDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Lynne MayneDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Philippe CollasDepartment of Molecular Medicine, Institute of Basic Medical Sciences, Faculty of Medicine, and Norwegian Center for Stem Cell Research, University of Oslo, 0317 Oslo, Norway.
Jeffrey R MannDepartment of Anatomy and Developmental Biology, Monash University, Clayton, Victoria 3800, Australia.
Lee H WongDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia lee.wong@monash.edu.
Monash University · AUUniversity of Melbourne · AUUniversity of Oslo · NOUniversity of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to being a hallmark at active genes, histone variant H3.3 is deposited by ATRX at repressive chromatin regions, including the telomeres. It is unclear how H3.3 promotes heterochromatin assembly. We show that H3.3 is targeted for K9 trimethylation to establish a heterochromatic state enriched in trimethylated H3.3K9 at telomeres. In H3f3a(-/-) and H3f3b(-/-) mouse embryonic stem cells (ESCs), H3.3 deficiency results in reduced levels of H3K9me3, H4K20me3 and ATRX at telomeres. The H3f3b(-/-) cells show increased levels of telomeric damage and sister chromatid exchange (t-SCE) activity when telomeres are compromised by treatment with a G-quadruplex (G4) DNA binding ligand or by ASF1 depletion. Overexpression of wild-type H3.3 (but not a H3.3K9 mutant) in H3f3b(-/-) cells increases H3K9 trimethylation level at telomeres and represses t-SCE activity induced by a G4 ligand. This study demonstrates the importance of H3.3K9 trimethylation in heterochromatin formation at telomeres. It provides insights into H3.3 function in maintaining integrity of mammalian constitutive heterochromatin, adding to its role in mediating transcription memory in the genome.

Indexed as

Histone CodeAnimalsCells, CulturedDNA DamageGene DeletionHeterochromatinHistonesLysineMethylationMiceSister Chromatid ExchangeTelomereTranscription, GeneticHeterochromatinHistonesLysine

Identifiers

PMID26304540
PMCPMC4666390
OpenAlexW1845992880

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.