Work

Histone Deacetylase 3 Binds to and Regulates the Multifunctional Transcription Factor TFII-I

Year: 2003

Type: article

Abstract: 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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.m206528200

Authors: Yu-Der Wen, W. Douglas Cress, Ananda L. Roy, Edward Seto

Institutions: University of South Florida, Moffitt Cancer Center, Tufts University

Language: English

Topic: Histone Deacetylase Inhibitors Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: Moffitt Cancer Center, National Institutes of Health, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases