Reference - Detail
|Author||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.|
|Title||Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2.|
|Journal||Nat Struct Mol Biol|
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.
|MeSH||Acetylation Animals Base Sequence Cell Cycle Proteins / antagonists & inhibitors Cell Cycle Proteins / metabolism DNA / genetics DNA / metabolism HeLa Cells Histone Acetyltransferases / antagonists & inhibitors Histone Acetyltransferases / metabolism Histones / metabolism* Humans In Vitro Techniques Mice Molecular Chaperones / chemistry Molecular Chaperones / genetics Molecular Chaperones / metabolism Nucleosomes / metabolism Protein Binding Protein Structure, Tertiary Recombinant Proteins / chemistry Recombinant Proteins / genetics Recombinant Proteins / metabolism Repressor Proteins / chemistry Repressor Proteins / genetics Repressor Proteins / metabolism* Sequence Deletion Transcription Factors / antagonists & inhibitors Transcription Factors / metabolism p300-CBP Transcription Factors|
|WOS Category||BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY|
|DNA material||pcDNA4-mmJDP2_wt (RDB04755) pGST-mmJDP2_full (RDB04757).|