Differential distribution of unmodified and phosphorylated histone deacetylase 2 in chromatin.

Histone deacetylase 2 (HDAC2) is one of the histone-modifying enzymes that regulate gene expression by remodeling chromatin structure. Along with HDAC1, HDAC2 is found in the Sin3 and NuRD multiprotein complexes, which are recruited to promoters by DNA-binding proteins. In this study, we show that the majority of HDAC2 in ...
human breast cancer cells is not phosphorylated. However, the minor population of HDAC2, preferentially cross-linked to DNA by cisplatin, is mono-, di-, or tri-phosphorylated. Furthermore, HDAC2 phosphorylation is required for formation of Sin3 and NuRD complexes and recruitment to promoters by transcription factors including p53, Rb, YY1, NF-kappaB, Sp1, and Sp3. Unmodified HDAC2 requires linker DNA to associate with chromatin but is not cross-linked to DNA by formaldehyde. We provide evidence that unmodified HDAC2 is associated with the coding region of transcribed genes, whereas phosphorylated HDAC2 is primarily recruited to promoters.
Mesh Terms:
Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, Chickens, Chromatin, Cross-Linking Reagents, DNA, DNA-Binding Proteins, Formaldehyde, Globins, Histone Deacetylase 2, Histone Deacetylases, Humans, Molecular Sequence Data, Nuclear Proteins, Phosphorylation, Promoter Regions, Genetic, Repressor Proteins, Retinoblastoma-Binding Protein 4, Transcription Factors
J. Biol. Chem.
Date: Nov. 09, 2007
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