Evidence map›Paper›PMID 29685391›Full record

ArticleBiophysical journal2018

Interactions of HP1 Bound to H3K9me3 Dinucleosome by Molecular Simulations and Biochemical Assays.

Shuhei Watanabe, Yuichi Mishima, Masahiro Shimizu, Isao Suetake, Shoji Takada

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 52 citations in OpenAlex.

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  14. Genome modeling: From chromatin fibers to genes.Current opinion in structural biology · 2023
    Review
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  18. Skin Aging, Cellular Senescence and Natural Polyphenols.International journal of molecular sciences · 2021
    Review
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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 3 institutions in 1 country.

Shuhei WatanabeDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa, Sakyo, Kyoto, Japan.
Yuichi MishimaInstitute for Protein Research, Osaka University, Suita, Osaka, Japan.
Masahiro ShimizuDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa, Sakyo, Kyoto, Japan.
Isao SuetakeInstitute for Protein Research, Osaka University, Suita, Osaka, Japan; College of Nutrition, Koshien University, Takarazuka, Japan. Electronic address: hotsuetake@hotmail.com.
Shoji TakadaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa, Sakyo, Kyoto, Japan. Electronic address: takada@biophys.kyoto-u.ac.jp.
Kyoto University · JPOsaka University · JPProtein Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterochromatin protein 1 (HP1), associated with heterochromatin formation, recognizes an epigenetically repressive marker, trimethylated lysine 9 in histone H3 (H3K9me3), and generally contributes to long-term silencing. How HP1 induces heterochromatin is not fully understood. Recent experiments suggested that not one, but two nucleosomes provide a platform for this recognition. Integrating previous and new biochemical assays with computational modeling, we provide near-atomic structural models for HP1 binding to the dinucleosomes. We found that the dimeric HP1α tends to bind two H3K9me3s that are in adjacent nucleosomes, thus bridging two nucleosomes. We identified, to our knowledge, a novel DNA binding motif in the hinge region that is specific to HP1α and is essential for recognizing the H3K9me3 sites of two nucleosomes. An HP1 isoform, HP1γ, does not easily bridge two nucleosomes in extended conformations because of the absence of the above binding motif and its shorter hinge region. We propose a molecular mechanism for chromatin structural changes caused by HP1.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHistonesLysineMethylationNucleosomesProtein BindingProtein ConformationChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHistonesLysineNucleosomes

Identifiers

PMID29685391
PMCPMC6129468
OpenAlexW2800637891

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.