Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2.

Article Details

Citation

Jin C, Kato K, Chimura T, Yamasaki T, Nakade K, Murata T, Li H, Pan J, Zhao M, Sun K, Chiu R, Ito T, Nagata K, Horikoshi M, Yokoyama KK

Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2.

Nat Struct Mol Biol. 2006 Apr;13(4):331-8. Epub 2006 Mar 5.

PubMed ID
16518400 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Jun dimerization protein 2Q8WYK2Details