Evidence map›Paper›PMID 37941146›Full record

ArticleNucleic acids research2023

Structural basis for the allosteric regulation and dynamic assembly of DNMT3B.

Jiuwei Lu, Jian Fang, Hongtao Zhu, Kimberly Lu Liang, Nelli Khudaverdyan, Jikui Song

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Multidomain interaction governs the filamentous assembly of the dominant-negative DNMT3A R882H mutant.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Differentiation of mtDNA Methylation in Tissues of Ridgetail White Prawn,Animals : an open access journal from MDPI · 2025
    Article
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  11. 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

6 authors at 2 institutions in 1 country.

Jiuwei LuDepartment of Biochemistry, University of California, Riverside, CA92521, USA.ORCID 0000-0002-6478-4081
Jian FangDepartment of Biochemistry, University of California, Riverside, CA92521, USA.
Hongtao ZhuVollum Institute, Oregon Health and Science University, Portland, OR, USA.
Kimberly Lu LiangDiamond Bar High School, Diamon Bar, CA91765, USA.
Nelli KhudaverdyanDepartment of Biochemistry, University of California, Riverside, CA92521, USA.
Jikui SongDepartment of Biochemistry, University of California, Riverside, CA92521, USA.ORCID 0000-0002-4958-1032
University of California, Riverside · USOregon Health & Science University · US

Funding

WORK ORDER 126643 B539 EXPAND IC SUITE75N91019D00024 · NIAID · LEIDOS BIOMEDICAL RESEARCH, INC. · PI BRISCOE, LYNN · 2019 to 2025
$3932.6M
The Stanford-SLAC CryoEM Center supplementU24GM129541 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH, HEDMAN, BRITT · 2018 to 2023
$54.8M
Mechanistic Insights into Mammalian DNA MethylationR35GM119721 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI Jikui Song · 2016 to 2026
$5.3M
NCI NIH HHS 75N91019D00024NIGMS NIH HHS R35 GM119721NIGMS NIH HHS U24 GM129541NIH HHS R35GM119721
6 · The paper itself

Abstract

Oligomerization of DNMT3B, a mammalian de novo DNA methyltransferase, critically regulates its chromatin targeting and DNA methylation activities. However, how the N-terminal PWWP and ADD domains interplay with the C-terminal methyltransferase (MTase) domain in regulating the dynamic assembly of DNMT3B remains unclear. Here, we report the cryo-EM structure of DNMT3B under various oligomerization states. The ADD domain of DNMT3B interacts with the MTase domain to form an autoinhibitory conformation, resembling the previously observed DNMT3A autoinhibition. Our combined structural and biochemical study further identifies a role for the PWWP domain and its associated ICF mutation in the allosteric regulation of DNMT3B tetramer, and a differential functional impact on DNMT3B by potential ADD-H3K4me0 and PWWP-H3K36me3 bindings. In addition, our comparative structural analysis reveals a coupling between DNMT3B oligomerization and folding of its substrate-binding sites. Together, this study provides mechanistic insights into the allosteric regulation and dynamic assembly of DNMT3B.

Indexed as

DNA Methyltransferase 3BAllosteric RegulationChromatinCryoelectron MicroscopyDNA (Cytosine-5-)-MethyltransferasesDNA MethylationDNA Methyltransferase 3AHumansMammalsChromatinDNA (Cytosine-5-)-MethyltransferasesDNA Methyltransferase 3ADNA Methyltransferase 3BDNMT3B protein, human

Identifiers

PMID37941146
PMCPMC10711551
OpenAlexW4388539739

What Socratic 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 Socratic graph.