Mechanisms of DNA methyltransferase 3A1-mediated DNA methylation of nucleosomes.

Ethan Ward, Drew McDonald, Tyler Holl, Norbert Reich

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in

0citing 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

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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

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors.

Ethan WardDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.

Drew McDonaldDepartment of Biomolecular Science and Engineering, University of California, Santa Barbara, California, USA.

Tyler HollDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA.

Norbert ReichDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California, USA; Department of Biomolecular Science and Engineering, University of California, Santa Barbara, California, USA. Electronic address: reich@chem.ucsb.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA methyltransferase 3A1 (DNMT3A1) plays a crucial role in establishing DNA methylation patterns that regulate gene expression and drive cellular differentiation. In this study, we investigated the biochemical mechanisms underlying DNMT3A1's interactions with nucleosomes, the fundamental units of chromatin. Using radiochemical activity assays, along with fluorescence anisotropy and AlphaLISA binding assays, we demonstrated that DNMT3A1 has multivalent interactions with nucleosomes, binding linker DNA and nucleosome cores. Nanopore-based 5mC sequencing revealed that DNMT3A1 interactions with the nucleosome stimulate methylation of linker DNA up to 24 bp away from the nucleosome core. Additionally, our results indicate that DNMT3A1 binding is restricted to a single nucleosome, suggesting that its activity is not allosterically regulated by unattached nucleosomes. Together, these findings provide new mechanistic insights into how DNMT3A1 engages nucleosomes.

Indexed as

DNA (Cytosine-5-)-MethyltransferasesDNA MethylationNucleosomesAnimalsDNADNA Methyltransferase 3AHumansDNADNA (Cytosine-5-)-MethyltransferasesDNA Methyltransferase 3ANucleosomesDNA enzymeDNA methylationenzyme kineticsenzyme mechanismepigeneticsmultivalentnucleosome

Identifiers

PMID41724383

DOI10.1016/j.jbc.2026.111303

PMCPMC13015722

What OpenQuestion holds

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LicenceCC BY

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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.