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Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast

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  • Soyun Lee

    (Korea Advanced Institute of Science and Technology)

  • Seunghee Oh

    (Korea Advanced Institute of Science and Technology)

  • Kwiwan Jeong

    (Biocenter, Gyeonggi Business & Science Accelerator)

  • Hyelim Jo

    (Korea Advanced Institute of Science and Technology)

  • Yoonjung Choi

    (Korea Advanced Institute of Science and Technology)

  • Hogyu David Seo

    (Korea Advanced Institute of Science and Technology)

  • Minhoo Kim

    (Korea Advanced Institute of Science and Technology)

  • Joonho Choe

    (Korea Advanced Institute of Science and Technology)

  • Chang Seob Kwon

    (Korea Science Academy of KAIST)

  • Daeyoup Lee

    (Korea Advanced Institute of Science and Technology)

Abstract

Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2–Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions.

Suggested Citation

  • Soyun Lee & Seunghee Oh & Kwiwan Jeong & Hyelim Jo & Yoonjung Choi & Hogyu David Seo & Minhoo Kim & Joonho Choe & Chang Seob Kwon & Daeyoup Lee, 2018. "Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-017-02759-8
    DOI: 10.1038/s41467-017-02759-8
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    Cited by:

    1. Fei He & Qi Yu & Min Wang & Rongsha Wang & Xuanyunjing Gong & Feng Ge & Xilan Yu & Shanshan Li, 2022. "SESAME-catalyzed H3T11 phosphorylation inhibits Dot1-catalyzed H3K79me3 to regulate autophagy and telomere silencing," Nature Communications, Nature, vol. 13(1), pages 1-20, December.

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