Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2


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 histones in vitro and in 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 activity in 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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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.).

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Correspondence to Kazunari K Yokoyama.

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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)

Supplementary Methods (PDF 62 kb)

Supplementary Data (PDF 135 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 Biol 13, 331–338 (2006).

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