Graduate School of Frontier Biosciences, Osaka University

Japanese

Genetically encoded system to track histone modification in vivo.

Journal Sci Rep 3, 2436 (2013)
Authors Yuko Sato (1, 2), Masanori Mukai (3), Jun Ueda (4), Michiko Muraki (5), Timothy J. Stasevich (1), Naoki Horikoshi (6), Tomoya Kujirai (6), Hiroaki Kita (3), Taisuke Kimura (3), Seiji Hira (3), Yasushi Okada (7), Yoko Hayashi-Takanaka (1, 2), Chikashi Obuse (8), Hitoshi Kurumizaka (6), Atsuo Kawahara (5), Kazuo Yamagata (4), Naohito Nozaki (9) & Hiroshi Kimura (1, 2)

  1. Graduate School of Frontier Biosciences, Osaka University, Suita. 565-0871, Japan
  2. JST, CREST, Suita. 565-0871, Japan
  3. Faculty of Science and Engineering and Graduate School of Natural Science, Konan University, Okamoto, Higashinada, Kobe 658-8501, Japan
  4. Research Institute for Microbial Diseases, Osaka University, Suita, 565-0871, Japan
  5. Laboratory for Cardiovascular Molecular Dynamics, Riken Quantitative Biology Center (QBiC), Suita, Osaka 565-0874
  6. Graduate School of Advanced Science and Engineering, Waseda University, Tokyo 162-8480, Japan
  7. Laboratory for Cell Polarity Regulation, Riken Quantitative Biology Center (QBiC), Suita, Osaka 565-0874
  8. Graduate School of Life Science, Hokkaido University, Sapporo. 001-0021, Japan
  9. Mab Institute Inc., Sapporo. 001-0021, Japan
Title Genetically encoded system to track histone modification in vivo.
PubMed 23942372
Laboratory Nuclear Dynamics Group 〈Prof. Hiraoka〉
Abstract Post-translational histone modifications play key roles in gene regulation, development, and differentiation, but their dynamics in living organisms remain almost completely unknown. To address this problem, we developed a genetically encoded system for tracking histone modifications by generating fluorescent modification-specific intracellular antibodies (mintbodies) that can be expressed in vivo. To demonstrate, an H3 lysine 9 acetylation specific mintbody (H3K9ac-mintbody) was engineered and stably expressed in human cells. In good agreement with the localization of its target acetylation, H3K9ac-mintbody was enriched in euchromatin, and its kinetics measurably changed upon treatment with a histone deacetylase inhibitor. We also generated transgenic fruit fly and zebrafish stably expressing H3K9ac-mintbody for in vivo tracking. Dramatic changes in H3K9ac-mintbody localization during Drosophila embryogenesis could highlight enhanced acetylation at the start of zygotic transcription around mitotic cycle 7. Together, this work demonstrates the broad potential of mintbody and lays the foundation for epigenetic analysis in vivo.