Evidence map›Paper›PMID 33479126›Full record

ArticleScience (New York, N.Y.)2021

Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation.

Marco Igor Valencia-Sánchez, Pablo De Ioannes, Miao Wang, David M Truong, Rachel Lee, Jean-Paul Armache, Jef D Boeke, Karim-Jean Armache

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

56 citing papers in PubMed, 108 citations in OpenAlex.

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  15. Review
  16. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  17. Article
  18. Review
  19. Article
  20. Two-way feedback between chromatin compaction and histone modification state explainsProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Marco Igor Valencia-Sánchez *Skirball Institute of Biomolecular Medicine, Department of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY 10016, USA.ORCID https://orcid.org/0000-0002-7199-4546
Pablo De Ioannes *Skirball Institute of Biomolecular Medicine, Department of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY 10016, USA.ORCID https://orcid.org/0000-0003-1944-3912
Miao Wang *Skirball Institute of Biomolecular Medicine, Department of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY 10016, USA.ORCID https://orcid.org/0000-0002-9193-3142
David M TruongInstitute for Systems Genetics, Department of Biochemistry and Molecular Pharmacology, New York University Langone Health, New York, NY 10016, USA.ORCID https://orcid.org/0000-0002-5121-5111
Rachel LeeSkirball Institute of Biomolecular Medicine, Department of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY 10016, USA.ORCID https://orcid.org/0000-0003-2501-5973
Jean-Paul ArmacheDepartment of Biochemistry and Molecular Biology, The Huck Institutes of the Life Sciences, Pennsylvania State University, University Park, PA 16802, USA.ORCID https://orcid.org/0000-0001-9195-2282
Jef D BoekeInstitute for Systems Genetics, Department of Biochemistry and Molecular Pharmacology, New York University Langone Health, New York, NY 10016, USA.ORCID https://orcid.org/0000-0001-5322-4946
Karim-Jean ArmacheSkirball Institute of Biomolecular Medicine, Department of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY 10016, USA. karim-jean.armache@nyulangone.org.ORCID https://orcid.org/0000-0002-0890-9513
New York University · USNYU Langone Health · USPennsylvania State University · US

Funding

Structural and functional analysis of gene silencingR01GM115882 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ARMACHE, KARIM JEAN · 2015 to 2023
$3.4M
NIGMS NIH HHS R01 GM115882
6 · The paper itself

Abstract

Dot1 (disruptor of telomeric silencing-1), the histone H3 lysine 79 (H3K79) methyltransferase, is conserved throughout evolution, and its deregulation is found in human leukemias. Here, we provide evidence that acetylation of histone H4 allosterically stimulates yeast Dot1 in a manner distinct from but coordinating with histone H2B ubiquitination (H2BUb). We further demonstrate that this stimulatory effect is specific to acetylation of lysine 16 (H4K16ac), a modification central to chromatin structure. We provide a mechanism of this histone cross-talk and show that H4K16ac and H2BUb play crucial roles in H3K79 di- and trimethylation in vitro and in vivo. These data reveal mechanisms that control H3K79 methylation and demonstrate how H4K16ac, H3K79me, and H2BUb function together to regulate gene transcription and gene silencing to ensure optimal maintenance and propagation of an epigenetic state.

Indexed as

Chromatin Assembly and DisassemblyProtein Processing, Post-TranslationalAcetylationHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsNucleosomesProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDot1 protein, S cerevisiaeHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID33479126
PMCPMC8279004
OpenAlexW3123057917

What OpenQuestion holds

Textmetadata
LicenceTDM
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.