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Histone H3K23-specific acetylation by MORF is coupled to H3K14 acylation

Author

Listed:
  • Brianna J. Klein

    (University of Colorado School of Medicine)

  • Suk Min Jang

    (CHU de Québec-UL Research Center-Oncology Division)

  • Catherine Lachance

    (CHU de Québec-UL Research Center-Oncology Division)

  • Wenyi Mi

    (Van Andel Research Institute)

  • Jie Lyu

    (University of California, Irvine
    Baylor College of Medicine)

  • Shun Sakuraba

    (National Institutes for Quantum and Radiological Science and Technology)

  • Krzysztof Krajewski

    (The University of North Carolina School of Medicine)

  • Wesley W. Wang

    (Texas A&M University)

  • Simone Sidoli

    (University of Pennsylvania
    Department of Biochemistry, Albert Einstein College of Medicine)

  • Jiuyang Liu

    (University of Colorado School of Medicine)

  • Yi Zhang

    (University of Colorado School of Medicine)

  • Xiaolu Wang

    (Van Andel Research Institute)

  • Becka M. Warfield

    (University of Colorado School of Medicine)

  • Andrew J. Kueh

    (The Walter and Eliza Hall Institute of Medical Research)

  • Anne K. Voss

    (The Walter and Eliza Hall Institute of Medical Research)

  • Tim Thomas

    (The Walter and Eliza Hall Institute of Medical Research)

  • Benjamin A. Garcia

    (University of Pennsylvania)

  • Wenshe R. Liu

    (Texas A&M University)

  • Brian D. Strahl

    (The University of North Carolina School of Medicine)

  • Hidetoshi Kono

    (National Institutes for Quantum and Radiological Science and Technology)

  • Wei Li

    (University of California, Irvine
    Baylor College of Medicine)

  • Xiaobing Shi

    (Van Andel Research Institute)

  • Jacques Côté

    (CHU de Québec-UL Research Center-Oncology Division)

  • Tatiana G. Kutateladze

    (University of Colorado School of Medicine)

Abstract

Acetylation of histone H3K23 has emerged as an essential posttranslational modification associated with cancer and learning and memory impairment, yet our understanding of this epigenetic mark remains insufficient. Here, we identify the native MORF complex as a histone H3K23-specific acetyltransferase and elucidate its mechanism of action. The acetyltransferase function of the catalytic MORF subunit is positively regulated by the DPF domain of MORF (MORFDPF). The crystal structure of MORFDPF in complex with crotonylated H3K14 peptide provides mechanistic insight into selectivity of this epigenetic reader and its ability to recognize both histone and DNA. ChIP data reveal the role of MORFDPF in MORF-dependent H3K23 acetylation of target genes. Mass spectrometry, biochemical and genomic analyses show co-existence of the H3K23ac and H3K14ac modifications in vitro and co-occupancy of the MORF complex, H3K23ac, and H3K14ac at specific loci in vivo. Our findings suggest a model in which interaction of MORFDPF with acylated H3K14 promotes acetylation of H3K23 by the native MORF complex to activate transcription.

Suggested Citation

  • Brianna J. Klein & Suk Min Jang & Catherine Lachance & Wenyi Mi & Jie Lyu & Shun Sakuraba & Krzysztof Krajewski & Wesley W. Wang & Simone Sidoli & Jiuyang Liu & Yi Zhang & Xiaolu Wang & Becka M. Warfi, 2019. "Histone H3K23-specific acetylation by MORF is coupled to H3K14 acylation," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12551-5
    DOI: 10.1038/s41467-019-12551-5
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    Cited by:

    1. Dustin C. Becht & Brianna J. Klein & Akinori Kanai & Suk Min Jang & Khan L. Cox & Bing-Rui Zhou & Sabrina K. Phanor & Yi Zhang & Ruo-Wen Chen & Christopher C. Ebmeier & Catherine Lachance & Maxime Gal, 2023. "MORF and MOZ acetyltransferases target unmethylated CpG islands through the winged helix domain," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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