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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.

Pubmed ID: 12393887

Authors

  • Wen YD
  • Cress WD
  • Roy AL
  • Seto E

Journal

The Journal of biological chemistry

Publication Data

January 17, 2003

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI45150
  • Agency: NIGMS NIH HHS, Id: GM58486

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Fluorescent Antibody Technique, Indirect
  • Histone Deacetylases
  • Molecular Sequence Data
  • Protein Binding
  • Transcription Factors, TFII