Evidence map›Paper›PMID 35739357›Full record

ArticleNature chemical biology2022

H2B Lys34 Ubiquitination Induces Nucleosome Distortion to Stimulate Dot1L Activity.

Huasong Ai, Maoshen Sun, Aijun Liu, Zixian Sun, Tingting Liu, Lin Cao, Lujun Liang, Qian Qu, Zichen Li, Zhiheng Deng and 8 more

Abstract read
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In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

35 citing papers in PubMed, 111 citations in OpenAlex.

  1. Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  2. Histone modification cross talk between a host and pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Review
  8. The molecular basis of lamin-specific chromatin interactions.Nature structural & molecular biology · 2025
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Cryo-EM Structures of Native Chromatin Units From Human Cells.Genes to cells : devoted to molecular & cellular mechanisms · 2025
    Article
  14. Review
  15. Article
  16. Article
  17. Article
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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

18 authors at 6 institutions in 1 country.

Huasong Ai *Department of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0002-3378-5874
Maoshen Sun *Department of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0002-8602-4817
Aijun Liu *MOE Key Laboratory of Protein Science, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, China.
Zixian Sun *MOE Key Laboratory of Protein Science, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, China.
Tingting Liu *iHuman Institute, ShanghaiTech University, Shanghai, China.
Lin CaoMOE Key Laboratory of Protein Science, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, China.
Lujun LiangDepartment of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.
Qian QuDepartment of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.
Zichen LiDepartment of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.
Zhiheng DengDepartment of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.
Zebin TongDepartment of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.
Guochao ChuDepartment of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China.
Xiaolin TianMOE Key Laboratory of Bioinformatics, School of Life Sciences, Tsinghua University, Beijing, China.
Haiteng DengMOE Key Laboratory of Bioinformatics, School of Life Sciences, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0001-9496-1280
Suwen ZhaoiHuman Institute, ShanghaiTech University, Shanghai, China.ORCID http://orcid.org/0000-0001-5609-434X
Jia-Bin LiCollege of Pharmaceutical Sciences, Soochow University, Suzhou, China. lijiabin@ustc.edu.cn.ORCID http://orcid.org/0000-0002-5308-5787
Zhiyong LouMOE Key Laboratory of Protein Science, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, China. louzy@mail.tsinghua.edu.cn.ORCID http://orcid.org/0000-0003-2728-881X
Lei LiuDepartment of Chemistry, Tsinghua-Peking Joint Center for Life Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Tsinghua University, Beijing, China. lliu@mail.tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-6290-8602
Center for Life Sciences · CNTsinghua University · CNShanghaiTech University · CNChinese University of Hong Kong, Shenzhen · CNNankai University · CNSoochow University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination-dependent histone crosstalk plays critical roles in chromatin-associated processes and is highly associated with human diseases. Mechanism studies of the crosstalk have been of the central focus. Here our study on the crosstalk between H2BK34ub and Dot1L-catalyzed H3K79me suggests a novel mechanism of ubiquitination-induced nucleosome distortion to stimulate the activity of an enzyme. We determined the cryo-electron microscopy structures of Dot1L-H2BK34ub nucleosome complex and the H2BK34ub nucleosome alone. The structures reveal that H2BK34ub induces an almost identical orientation and binding pattern of Dot1L on nucleosome as H2BK120ub, which positions Dot1L for the productive conformation through direct ubiquitin-enzyme contacts. However, H2BK34-anchored ubiquitin does not directly interact with Dot1L as occurs in the case of H2BK120ub, but rather induces DNA and histone distortion around the modified site. Our findings establish the structural framework for understanding the H2BK34ub-H3K79me trans-crosstalk and highlight the diversity of mechanisms for histone ubiquitination to activate chromatin-modifying enzymes.

Indexed as

HistonesNucleosomesChromatinCryoelectron MicroscopyHistone-Lysine N-MethyltransferaseHumansUbiquitinUbiquitinationChromatinDOT1L protein, humanHistone-Lysine N-MethyltransferaseHistonesNucleosomesUbiquitin

Identifiers

PMID35739357
OpenAlexW4283331244

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Registered trials

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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.