Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I.
Histone deacetylase 3 (HDAC3) is one of four members of the human class I histone deacetylases that are implicated in transcriptional repression through deacetylation of acetyllysines in amino-terminal tails of core histones. In an immunoaffinity purification using anti-HDAC3, transcription factor TFII-I copurified with HDAC3. Specificity of the HDAC3-TFII-I interaction was ... confirmed by coimmunoprecipitation of epitope-tagged proteins, GST pull-down assays, and protein colocalization with indirect immunofluorescence. An anti-TFII-I immunoprecipitate contained histone deacetylase enzymatic activity. Mutational analyses revealed that the carboxyl-terminal of HDAC3 (residues 373-401) and residues 363-606 of TFII-I were required for the HDAC3-TFII-I interaction. Transcriptional activation by TFII-I was severely reduced by overexpression of HDAC3. These results suggest that HDAC3 modulates some of the functions of TFII-I and provides a link between histone deacetylase and a multifunctional transcriptional activator.
Mesh Terms:
Amino Acid Sequence, Animals, COS Cells, Fluorescent Antibody Technique, Indirect, Histone Deacetylases, Molecular Sequence Data, Protein Binding, Transcription Factors, TFII
Amino Acid Sequence, Animals, COS Cells, Fluorescent Antibody Technique, Indirect, Histone Deacetylases, Molecular Sequence Data, Protein Binding, Transcription Factors, TFII
J. Biol. Chem.
Date: Jan. 17, 2003
PubMed ID: 12393887
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