Evidence map›Paper›PMID 26792892›Full record

ArticleNucleic acids research2016

Histone H3K36 trimethylation is essential for multiple silencing mechanisms in fission yeast.

Shota Suzuki, Hiroaki Kato, Yutaka Suzuki, Yuji Chikashige, Yasushi Hiraoka, Hiroshi Kimura, Koji Nagao, Chikashi Obuse, Shinya Takahata, Yota Murakami

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 60 citations in OpenAlex.

  1. Epigenetic regulation of transgenes.Journal of biotechnology · 2026
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  8. Class I histone deacetylase complex: Structure and functional correlates.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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

10 authors at 7 institutions in 1 country.

Shota SuzukiGraduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-0810, Japan.
Hiroaki KatoDepartment of Biochemistry, Shimane University School of Medicine, Izumo 693-8501, Japan PRESTO, Japan Science and Technology Agency (JST), 4-1-8 Honcho Kawaguchi 332-0012, Japan.
Yutaka SuzukiGraduate School of Frontier Sciences, University of Tokyo, Kashiwa 277-8562, Japan.
Yuji ChikashigeAdvanced ICT Research Institute, National Institute of Information and Communications Technology, Kobe 651-2492, Japan.
Yasushi HiraokaGraduate School of Frontier Biosciences, Osaka University, Suita 565-0871, Japan.
Hiroshi KimuraGraduate School of Frontier Biosciences, Osaka University, Suita 565-0871, Japan Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
Koji NagaoGraduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan.
Chikashi ObuseGraduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan.
Shinya TakahataGraduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-0810, Japan Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, Japan.
Yota MurakamiGraduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-0810, Japan Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060-0810, Japan yota@sci.hokudai.ac.jp.ORCID 0000-0002-2023-1303
Hokkaido University · JPHokkaido University of Science · JPNational Institute of Information and Communications Technology · JPShimane University · JPThe University of Osaka · JPThe University of Tokyo · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In budding yeast, Set2 catalyzes di- and trimethylation of H3K36 (H3K36me2 and H3K36me3) via an interaction between its Set2-Rpb1 interaction (SRI) domain and C-terminal repeats of RNA polymerase II (Pol2) phosphorylated at Ser2 and Ser5 (CTD-S2,5-P). H3K36me2 is sufficient for recruitment of the Rpd3S histone deacetylase complex to repress cryptic transcription from transcribed regions. In fission yeast, Set2 is also responsible for H3K36 methylation, which represses a subset of RNAs including heterochromatic and subtelomeric RNAs, at least in part via recruitment of Clr6 complex II, a homolog of Rpd3S. Here, we show that CTD-S2P-dependent interaction of fission yeast Set2 with Pol2 via the SRI domain is required for formation of H3K36me3, but not H3K36me2. H3K36me3 silenced heterochromatic and subtelomeric transcripts mainly through post-transcriptional and transcriptional mechanisms, respectively, whereas H3K36me2 was not enough for silencing. Clr6 complex II appeared not to be responsible for heterochromatic silencing by H3K36me3. Our results demonstrate that H3K36 methylation has multiple outputs in fission yeast; these findings provide insights into the distinct roles of H3K36 methylation in metazoans, which have different enzymes for synthesis of H3K36me1/2 and H3K36me3.

Indexed as

Gene Expression Regulation, FungalGene SilencingProtein Processing, Post-TranslationalChromosomes, FungalGenes, FungalHeterochromatinHistone-Lysine N-MethyltransferaseHistonesMethylationProtein Interaction Domains and MotifsRNA Polymerase IIRNA StabilitySchizosaccharomycesSchizosaccharomyces pombe ProteinsTelomereTranscription, GeneticHeterochromatinHistone-Lysine N-MethyltransferaseHistonesRNA Polymerase IISchizosaccharomyces pombe ProteinsSet2 protein, S pombe

Identifiers

PMID26792892
PMCPMC4872076
OpenAlexW2301971638

What OpenQuestion holds

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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.