title: Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2.
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.
authors.affiliation: Gene Engineering Division, Dept. of Biological Systems, BioResource Center, RIKEN (The Institute of Physical & Chemical Research), Tsukuba Science City, Ibaraki 305-0074, Japan.
authors.forename: Chunyuan
authors.initials: C
authors.lastname: Jin
authors.forename: Kohsuke
authors.initials: K
authors.lastname: Kato
authors.forename: Takahiko
authors.initials: T
authors.lastname: Chimura
authors.forename: Takahito
authors.initials: T
authors.lastname: Yamasaki
authors.forename: Koji
authors.initials: K
authors.lastname: Nakade
authors.forename: Takehide
authors.initials: T
authors.lastname: Murata
authors.forename: Hongjie
authors.initials: H
authors.lastname: Li
authors.forename: Jianzhi
authors.initials: J
authors.lastname: Pan
authors.forename: Mujun
authors.initials: M
authors.lastname: Zhao
authors.forename: Kailai
authors.initials: K
authors.lastname: Sun
authors.forename: Robert
authors.initials: R
authors.lastname: Chiu
authors.forename: Takashi
authors.initials: T
authors.lastname: Ito
authors.forename: Kyosuke
authors.initials: K
authors.lastname: Nagata
authors.forename: Masami
authors.initials: M
authors.lastname: Horikoshi
authors.forename: Kazunari K
authors.initials: KK
authors.lastname: Yokoyama
mesh_terms: D000107:Acetylation; D000818:Animals; D001483:Base Sequence; D018797:Cell Cycle Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D004247:DNA / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D051548:Histone Acetyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D051379:Mice; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion; D014157:Transcription Factors / Q000037:antagonists & inhibitors / Q000378:metabolism; D050880:p300-CBP Transcription Factors; D000099224:p300-CBP-Associated Factor
chemical_list: D018797:Cell Cycle Proteins; D004247:DNA; D051548:Histone Acetyltransferases; D006657:Histones; D018832:Molecular Chaperones; D009707:Nucleosomes; D011994:Recombinant Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D050880:p300-CBP Transcription Factors; D000099224:p300-CBP-Associated Factor; C491386:Jundp2 protein, mouse