RRC ID 1902
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
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.
Volume 13(4)
Pages 331-8
Published 2006-4-1
DOI 10.1038/nsmb1063
PII nsmb1063
PMID 16518400
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
IF 11.98
Times Cited 55
DNA material pcDNA4-mmJDP2_wt (RDB04755) pGST-mmJDP2_full (RDB04757).