Mechanism of SMRT Corepressor Recruitment by the BCL6 BTB Domain

K. Farid Ahmad, Ari Melnick, Stuart Lax, Denis Bouchard, Jun Liu, Chih Li Kiang, Sebastian Mayer, Shinichiro Takahashi, Jonathan D. Licht, Gilbert G. Privé

Research output: Contribution to journalArticlepeer-review

229 Scopus citations

Abstract

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 Å. 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.

Original languageEnglish
Pages (from-to)1551-1564
Number of pages14
JournalMolecular Cell
Volume12
Issue number6
DOIs
StatePublished - Dec 2003

Fingerprint

Dive into the research topics of 'Mechanism of SMRT Corepressor Recruitment by the BCL6 BTB Domain'. Together they form a unique fingerprint.

Cite this