TitleMechanism of SMRT corepressor recruitment by the BCL6 BTB domain.
Publication TypeJournal Article
Year of Publication2003
AuthorsK Ahmad, Farid, Melnick Ari, Lax Stuart, Bouchard Denis, Liu Jun, Kiang Chih-Li, Mayer Sebastian, Takahashi Shinichiro, Licht Jonathan D., and Prive Gilbert G.
JournalMol Cell
Date Published2003 Dec
KeywordsAmino Acid Sequence, Crystallography, X-Ray, DNA-Binding Proteins, Gene Expression Regulation, Humans, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, Molecular Structure, Multiprotein Complexes, Nuclear Receptor Co-Repressor 2, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-bcl-6, Recombinant Fusion Proteins, Repressor Proteins, Sequence Alignment, Transcription Factors

<p>BCL6 encodes a transcription factor that represses genes necessary for the terminal differentiation of lymphocytes within germinal centers, and the misregulated expression of this factor is strongly implicated in several types of B cell lymphoma. The homodimeric BTB domain of BCL6 (also known as the POZ domain) is required for the repression activity of the protein and interacts directly with the SMRT and N-CoR corepressors that are found within large multiprotein histone deacetylase-containing complexes. We have identified a 17 residue fragment from SMRT that binds to the BCL6 BTB domain, and determined the crystal structure of the complex to 2.2 A. Two SMRT fragments bind symmetrically to the BCL6 BTB homodimer and, in combination with biochemical and in vivo data, the structure provides insight into the basis of transcriptional repression by this critical B cell lymphoma protein.</p>

Alternate JournalMol Cell
PubMed ID14690607
Grant ListCA 59936 / CA / NCI NIH HHS / United States
R21 CA 99982 / CA / NCI NIH HHS / United States