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Nature Structural & Molecular Biology
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Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2

Nature Structural & Molecular Biologyvolume 13, pages331–338 (2006)Cite this article

Abstract

Jun dimerization protein-2 (JDP2) is a component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Here, we examine the functional mechanisms of JDP2 and show that it can inhibit p300-mediated acetylation of core histonesin vitro andin vivo. Inhibition of histone acetylation requires the N-terminal 35 residues and the DNA-binding region of JDP2. In addition, we demonstrate that JDP2 has histone-chaperone activityin vitro. These results suggest that the sequence-specific DNA-binding protein JDP2 may control transcription via direct regulation of the modification of histones and the assembly of chromatin.

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Figure 1: Inhibition by JDP2 of histone acetylation.
Figure 2: Interaction of JDP2 with histones.
Figure 3: Mapping of the histone-binding and HAT-inhibition domains of JDP2.
Figure 4: The histone-chaperone activity of JDP2.
Figure 5: Role of histone-binding and HAT-inhibition activities of JDP2 in transcription and differentiation of F9 cells.

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Acknowledgements

The authors thank V. Calhoun, K. Itakura, G. Gachelin, H. Ugai, Y. Shinozuka, M. Kimura, J. Svejstrup, K. Ura, J.L. Workman, K. Ikeda and G. Felsenfeld for reagents and/or many helpful discussions, suggestions and critical reading of the manuscript. This work was supported by grants from the RIKEN Bioresource Project and by a grant from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to K.K.Y.).

Author information

Author notes

  1. Chunyuan Jin

    Present address: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health, Bethesda, Maryland, 20892, USA

Authors and Affiliations

  1. Gene Engineering Division, Dept. of Biological Systems, BioResource Center, RIKEN (The Institute of Physical & Chemical Research), Tsukuba Science City, Ibaraki, 305-0074, Japan

    Chunyuan Jin, Takahito Yamasaki, Koji Nakade, Takehide Murata, Hongjie Li, Jianzhi Pan & Kazunari K Yokoyama

  2. Dept. of Medical Genetics, China Medical University, Shenyang, 110001, China

    Chunyuan Jin, Hongjie Li & Kailai Sun

  3. Dept. of Infection Biology, Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba, 305-8575, Japan

    Kohsuke Kato & Kyosuke Nagata

  4. Institute of Molecular & Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan

    Takahiko Chimura & Masami Horikoshi

  5. Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Science, Chinese Academy of Sciences, Shanghai, 20031, China

    Mujun Zhao

  6. Dental Research Institute, University of California at Los Angeles School of Medicine, Los Angeles, 90095-1668, California, USA

    Robert Chiu

  7. Dept. of Biochemistry, Nagasaki University School of Medicine, 1-24-4 Sakamoto, Nagasaki, 852-8523, Japan

    Takashi Ito

Authors
  1. Chunyuan Jin
  2. Kohsuke Kato
  3. Takahiko Chimura
  4. Takahito Yamasaki
  5. Koji Nakade
  6. Takehide Murata
  7. Hongjie Li
  8. Jianzhi Pan
  9. Mujun Zhao
  10. Kailai Sun
  11. Robert Chiu
  12. Takashi Ito
  13. Kyosuke Nagata
  14. Masami Horikoshi
  15. Kazunari K Yokoyama

Corresponding author

Correspondence toKazunari K Yokoyama.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Supplementary information

Supplementary Fig. 1

Characterization of the HAT assay (PDF 337 kb)

Supplementary Fig. 2

His-JDP2 has INHAT activity (PDF 244 kb)

Supplementary Fig. 3

Interactions between reconstituted mononucleosomes and JDP2 (PDF 225 kb)

Supplementary Fig. 4

The purity and stability of wild-type JDP2 and its derivatives (PDF 98 kb)

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Jin, C., Kato, K., Chimura, T.et al. Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2.Nat Struct Mol Biol13, 331–338 (2006). https://doi.org/10.1038/nsmb1063

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