Development and applications of genome editing and fluorescent imaging technologies toward precise epigenome editing

DOI
  • Nomura Wataru
    Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University

Bibliographic Information

Other Title
  • DNAメチル化制御から精密エピゲノム編集へ

Abstract

<p>Zinc finger (ZF) proteins consist of Cys2-His2-type modules composed of approximately 30 amino acids that adopt a ββα structure and coordinate a zinc ion. ZF domains recognizing specific DNA target sequences can substitute for the binding domains of various DNA-modifying enzymes to create designer nucleases, recombinases, and methyltransferases with programmable sequence specificity. Enzymatic genome editing and modification can be applied to many fields of basic research and medicine. The recent development of new platforms using transcription activator-like effector (TALE) proteins or the CRISPR-Cas9 system has expanded the range of possibilities for genome-editing technologies. These technologies empower investigators with the ability to efficiently knockout or regulate the functions of genes of interest by using as sequence-specific nucleases. In addition, these DNA binding domains can also be utilized to build a tool box for epigenetic controls by fusing with protein modification enzymes or DNA modification enzymes. In this review, overview of recent advancements of sequence-specific DNA binding domains and their applications for genome and epigenome editing technologies is described. Our research for epigenome editing including development of artificial zinc finger recombinase (ZFR), split DNA methyltransferase utilizing ZF domains for target recognition, and fluorescent imaging of histone proteins by ZIP tag-probe system are introduced. Advances in the ZF, TALE, and CRISPR-Cas9 platforms have paved the way for the next generation of genome/epigenome engineering approaches. Perspectives for the future of epigenome engineering are also discussed, including development of precisely controlled epigenome editing and regulation.</p>

Journal

  • MEDCHEM NEWS

    MEDCHEM NEWS 27 (4), 200-207, 2017-11-01

    The Pharmaceutical Society of Japan

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Details 詳細情報について

  • CRID
    1390001277399696000
  • NII Article ID
    130007755934
  • DOI
    10.14894/medchem.27.4_200
  • ISSN
    24328626
    24328618
  • Text Lang
    ja
  • Data Source
    • JaLC
    • CiNii Articles
    • KAKEN
  • Abstract License Flag
    Disallowed

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