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.

journal_name

Nat Struct Mol Biol

authors

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

doi

10.1038/nsmb1063

keywords:

subject

Has Abstract

pub_date

2006-04-01 00:00:00

pages

331-8

issue

4

eissn

1545-9993

issn

1545-9985

pii

nsmb1063

journal_volume

13

pub_type

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