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DNA-dependent conversion of Oct-1 and Oct-2 into transcriptional repressors by Groucho/TLE.

Nucleic acids research | Aug 16, 2005

POU domain proteins contain a bipartite DNA-binding element that can confer allosteric control of coactivator recruitment. Dimerization of Oct-1 and Oct-2 on palindromic response elements results in the conformational dependent inclusion or exclusion of the transcriptional coactivator OBF-1. In this paper, we demonstrate that Oct-1 and Oct-2 can function as transcriptional repressors by recruiting and physically interacting with members of the Grg/TLE family of corepressors. In accordance with a model of DNA induced cofactor assembly, and analogous to the recruitment of the OBF-1 coactivator, the different Grg/TLE members can discriminate between both Oct-1 and Oct-2, and the monomeric or dimeric nature of the POU/DNA complex.

Pubmed ID: 16103132 RIS Download

Mesh terms: Base Sequence | Basic Helix-Loop-Helix Transcription Factors | Binding Sites | Biological Evolution | Cell Line | DNA | DNA-Binding Proteins | Dimerization | Humans | Octamer Transcription Factor-1 | Protein Structure, Tertiary | Repressor Proteins | Response Elements | Transcription Factors | Transcriptional Activation