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 Bioljournal_title
Nature structural & molecular biologyauthors
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 KKdoi
10.1038/nsmb1063keywords:
subject
Has Abstractpub_date
2006-04-01 00:00:00pages
331-8issue
4eissn
1545-9993issn
1545-9985pii
nsmb1063journal_volume
13pub_type
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