Nature Structural & Molecular Biology 13, 331 - 338 (2006)
Published online: 5 March 2006; | doi:10.1038/nsmb1063
Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2Chunyuan Jin1, 2, 8, Kohsuke Kato3, Takahiko Chimura4, Takahito Yamasaki1, Koji Nakade1, Takehide Murata1, Hongjie Li1, 2, Jianzhi Pan1, Mujun Zhao5, Kailai Sun2, Robert Chiu6, Takashi Ito7, Kyosuke Nagata3, Masami Horikoshi4
& Kazunari K Yokoyama11
Gene Engineering Division, Dept. of Biological Systems, BioResource Center, RIKEN (The Institute of Physical & Chemical Research), Tsukuba Science City, Ibaraki 305-0074, Japan. 2
Dept. of Medical Genetics, China Medical University, Shenyang 110001, China. 3
Dept. of Infection Biology, Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba 305-8575, Japan. 4
Institute of Molecular & Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. 5
Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Science, Chinese Academy of Sciences, Shanghai 20031, China. 6
Dental Research Institute, University of California at Los Angeles School of Medicine, Los Angeles, California 90095-1668, USA. 7
Dept. of Biochemistry, Nagasaki University School of Medicine, 1-24-4 Sakamoto, Nagasaki 852-8523, Japan. 8
Present address: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health, Bethesda, Maryland 20892, USA.
Correspondence should be addressed to Kazunari K Yokoyama kazu@brc.riken.jp 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.
MORE ARTICLES LIKE THIS These links to content published by NPG are automatically generated.
|
