Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2

Nat Struct Mol Biol. 2006 Apr;13(4):331-8. doi: 10.1038/nsmb1063.

Chunyuan Jin ¹, Kohsuke Kato, Takahiko Chimura, Takahito Yamasaki, Koji Nakade, Takehide Murata, Hongjie Li, Jianzhi Pan, Mujun Zhao, Kailai Sun, Robert Chiu, Takashi Ito, Kyosuke Nagata, Masami Horikoshi, Kazunari K Yokoyama

Affiliations

Affiliation

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

PMID: 16518400 DOI: 10.1038/nsmb1063

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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