Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2

C Jin, K Kato, T Chimura, T Yamasaki… - Nature structural & …, 2006 - nature.com
C Jin, K Kato, T Chimura, T Yamasaki, K Nakade, T Murata, H Li, J Pan, M Zhao, K Sun…
Nature structural & molecular biology, 2006nature.com
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 …
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.
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