Evidence map›Paper›PMID 30325428›Full record

ArticleNucleic acids research2018

Crosstalk among Set1 complex subunits involved in H2B ubiquitylation-dependent H3K4 methylation.

Jongcheol Jeon, Robert K McGinty, Tom W Muir, Jung-Ae Kim, Jaehoon Kim

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Decoding RNF20: an epigenetic modifier and beyond.Frontiers in cell and developmental biology · 2026
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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

5 authors at 3 institutions in 2 countries.

Jongcheol JeonDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Robert K McGintyLaboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, NY 10065, USA.
Tom W MuirDepartment of Chemistry, Princeton University, Frick Laboratory, Princeton, NJ 08544, USA.
Jung-Ae KimPersonalized Genomic Medicine Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, South Korea.
Jaehoon KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Korea Advanced Institute of Science and Technology · KRPrinceton University · USRockefeller University · US

Funding

Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
Development and Applications of 'Designer Chromatin'R01GM107047 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2013 to 2016
$1.2M
NIGMS NIH HHS R01 GM107047NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

H2B ubiquitylation (H2Bub)-dependent H3K4 methylation is mediated by the multisubunit Set1 complex (Set1C) in yeast, but precisely how Set1C subunits contribute to this histone modification remains unclear. Here, using reconstituted Set1Cs and recombinant H2Bub chromatin, we identified Set1C subunits and domains involved in the H2Bub-dependent H3K4 methylation process, showing that the Spp1 PHDL domain, in conjunction with the Set1 n-SET domain, interacts with Swd1/Swd3 and that this interaction is essential for H2Bub-dependent H3K4 methylation. Importantly, Set1C containing an Spp1-Swd1 fusion bypasses the requirement for H2Bub for H3K4 methylation, suggesting that the role of H2Bub is to induce allosteric rearrangements of the subunit-interaction network within the active site of Set1C that are necessary for methylation activity. Moreover, the interaction between the Set1 N-terminal region and Swd1 renders the Spp1-lacking Set1C competent for H2Bub-dependent H3K4 methylation. Collectively, our results suggest that H2Bub induces conformational changes in Set1C that support H3K4 methylation activity.

Indexed as

Catalytic DomainChromatinHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesMethylationProtein BindingProtein MultimerizationProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationChromatinHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiae

Identifiers

PMID30325428
PMCPMC6265457
OpenAlexW2898044585

What OpenQuestion 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 OpenQuestion graph.