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 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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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.).
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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)
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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). https://doi.org/10.1038/nsmb1063
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DOI: https://doi.org/10.1038/nsmb1063
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