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
  • 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.