Evidence map›Paper›PMID 32472103›Full record

ArticleNature chemistry2020

In situ chromatin interactomics using a chemical bait and trap approach.

Antony J Burton, Michael Haugbro, Leah A Gates, John D Bagert, C David Allis, Tom W Muir

Abstract read
In one paragraph

Article in Nature chemistry, 2020. 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
–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

35 citing papers in PubMed.

  1. Review
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  12. DPF2 reads histone lactylation to drive transcription and tumorigenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. How chromatin senses plant hormones.Current opinion in plant biology · 2024
    Review
  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Antony J BurtonDepartment of Chemistry, Frick Chemistry Laboratory, Princeton University, Princeton, NJ, USA.ORCID http://orcid.org/0000-0002-2340-3262
Michael HaugbroDepartment of Chemistry, Frick Chemistry Laboratory, Princeton University, Princeton, NJ, USA.ORCID http://orcid.org/0000-0001-7797-8259
Leah A GatesLaboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY, USA.
John D BagertDepartment of Chemistry, Frick Chemistry Laboratory, Princeton University, Princeton, NJ, USA.
C David AllisLaboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, NY, USA.
Tom W MuirDepartment of Chemistry, Frick Chemistry Laboratory, Princeton University, Princeton, NJ, USA. muir@princeton.edu.ORCID http://orcid.org/0000-0001-9635-0344

Funding

Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
Structure, Function and Applications of InteinsR01GM086868 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2008 to 2025
$4.4M
Structure-activity relationships governing mammalian SWI/SNF chromatin remodeling activity as a function of chromatin stateR01CA259365 · NCI · DANA-FARBER CANCER INST · PI Cigall Kadoch, Tom Muir · 2021 to 2026
$4.2M
Exploring second-tier post-translational modifications in chromatin biology: A new class of histone modifications with undetermined functionF32GM123659 · NIGMS · PRINCETON UNIVERSITY · PI BAGERT, JOHN DAVID · 2017 to 2018
$118k
NCI NIH HHS P01 CA196539NCI NIH HHS R01 CA259365NIGMS NIH HHS F32 GM123659NIGMS NIH HHS R01 GM086868NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

Elucidating the physiological binding partners of histone post-translational modifications (hPTMs) is key to understanding fundamental epigenetic regulatory pathways. Determining such interactomes will enable the study of how perturbations of these interactions affect disease. Here we use a synthetic biology approach to set a series of hPTM-controlled photo-affinity traps in native chromatin. Using quantitative proteomics, the local interactomes of these chemically customized chromatin landscapes are determined. We show that the approach captures transiently interacting factors such as methyltransferases and demethylases, as well as previously reported and novel hPTM reader proteins. We also apply this in situ proteomics approach to a recently disclosed cancer-associated histone mutation, H3K4M, revealing a number of perturbed interactions with the mutated tail. Collectively our studies demonstrate that modifying and interrogating native chromatin with chemical precision is a powerful tool for exploring epigenetic regulation and dysregulation at the molecular level.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalChromatinHistone CodeHistone DemethylasesHistonesHumansMethyltransferasesMutationNeoplasmsPhotoaffinity LabelsProteomicsChromatinHistone DemethylasesHistonesMethyltransferasesPhotoaffinity Labels

Identifiers

PMID32472103
PMCPMC7331920

What OpenQuestion holds

Textmetadata
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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.