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

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Title: Histone H3K36 trimethylation is essential for multiple silencing mechanisms in fission yeast
Authors: Suzuki, Shota Browse this author
Kato, Hiroaki Browse this author
Suzuki, Yutaka Browse this author
Chikashige, Yuji Browse this author
Hiraoka, Yasushi Browse this author
Kimura, Hiroshi Browse this author
Nagao, Koji Browse this author
Obuse, Chikashi Browse this author
Takahata, Shinya Browse this author
Murakami, Yota Browse this author
Issue Date: 20-May-2016
Publisher: Oxford University Press
Journal Title: Nucleic acids research
Volume: 44
Issue: 9
Start Page: 4147
End Page: 4162
Publisher DOI: 10.1093/nar/gkw008
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 Ser(2) and Ser(5) (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.
Rights: https://creativecommons.org/licenses/by-nc/4.0/
Type: article
URI: http://hdl.handle.net/2115/62415
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 村上 洋太

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