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

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

Authors

  • Malin S
  • Linderson Y
  • Almqvist J
  • Ernberg I
  • Tallone T
  • Pettersson S

Journal

Nucleic acids research

Publication Data

August 16, 2005

Associated Grants

None

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