Evidence map›Paper›PMID 30923167›Full record

ArticleGenes & development2019

Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase.

Seongmin Jang, Chanshin Kang, Han-Sol Yang, Taeyang Jung, Hans Hebert, Ka Young Chung, Seung Joong Kim, Sungchul Hohng, Ji-Joon Song

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
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

51 citing papers in PubMed, 97 citations in OpenAlex.

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  10. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    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

9 authors at 4 institutions in 2 countries.

Seongmin JangDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
Chanshin KangDepartment of Physics and Astronomy, Seoul National University, Seoul 08826, Korea.
Han-Sol YangSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Taeyang JungSchool of Engineering Sciences in Chemistry, Biotechnology, and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, S-141 52 Huddinge, Sweden.
Hans HebertSchool of Engineering Sciences in Chemistry, Biotechnology, and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, S-141 52 Huddinge, Sweden.
Ka Young ChungSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Seung Joong KimDepartment of Physics, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
Sungchul HohngDepartment of Physics and Astronomy, Seoul National University, Seoul 08826, Korea.
Ji-Joon SongDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
Korea Advanced Institute of Science and Technology · KRKarolinska Institutet · SESeoul National University · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DOT1L is a histone H3 Lys79 methyltransferase whose activity is stimulated by histone H2B Lys120 ubiquitination, suggesting cross-talk between histone H3 methylation and H2B ubiquitination. Here, we present cryo-EM structures of DOT1L complexes with unmodified or H2B ubiquitinated nucleosomes, showing that DOT1L recognizes H2B ubiquitin and the H2A/H2B acidic patch through a C-terminal hydrophobic helix and an arginine anchor in DOT1L, respectively. Furthermore, the structures combined with single-molecule FRET experiments show that H2B ubiquitination enhances a noncatalytic function of the DOT1L-destabilizing nucleosome. These results establish the molecular basis of the cross-talk between H2B ubiquitination and H3 Lys79 methylation as well as nucleosome destabilization by DOT1L.

Indexed as

ArginineCatalytic DomainCryoelectron MicroscopyHistone-Lysine N-MethyltransferaseHistonesHumansHydrophobic and Hydrophilic InteractionsMethylationMethyltransferasesModels, MolecularNucleosomesProtein StabilityProtein Structure, SecondaryUbiquitinUbiquitinationArginineDOT1L protein, humanHistone-Lysine N-MethyltransferaseHistonesMethyltransferasesNucleosomesUbiquitincryo-EMhistonemethylationnucleosomeubiquitin

Identifiers

PMID30923167
PMCPMC6546062
OpenAlexW2907769723

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.