ASH1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin

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  • Vincent T Bicocca
    Institute of Molecular Biology, University of Oregon, Eugene, United States
  • Tereza Ormsby
    Department of Biochemistry Faculty of Science, Charles University, Prague, Czech Republic
  • Keyur K Adhvaryu
    St. George's University School of Medicine, Grenada, Caribbean
  • Shinji Honda
    Faculty of Medical Sciences, University of Fukui, Fukui, Japan
  • Eric U Selker
    Institute of Molecular Biology, University of Oregon, Eugene, United States

書誌事項

公開日
2018-11-23
資源種別
journal article
権利情報
  • http://creativecommons.org/licenses/by/4.0/
  • http://creativecommons.org/licenses/by/4.0/
  • http://creativecommons.org/licenses/by/4.0/
DOI
  • 10.7554/elife.41497
公開者
eLife Sciences Publications, Ltd

説明

<jats:p>Methylation of histone H3 at lysine 36 (H3K36me), a widely-distributed chromatin mark, largely results from association of the lysine methyltransferase (KMT) SET-2 with RNA polymerase II (RNAPII), but most eukaryotes also have additional H3K36me KMTs that act independently of RNAPII. These include the orthologs of ASH1, which are conserved in animals, plants, and fungi but whose function and control are poorly understood. We found that Neurospora crassa has just two H3K36 KMTs, ASH1 and SET-2, and were able to explore the function and distribution of each enzyme independently. While H3K36me deposited by SET-2 marks active genes, inactive genes are modified by ASH1 and its activity is critical for their repression. ASH1-marked chromatin can be further modified by methylation of H3K27, and ASH1 catalytic activity modulates the accumulation of H3K27me2/3 both positively and negatively. These findings provide new insight into ASH1 function, H3K27me2/3 establishment, and repression in facultative heterochromatin.</jats:p>

収録刊行物

  • eLife

    eLife 7 e41497-, 2018-11-23

    eLife Sciences Publications, Ltd

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