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Related Experiment Videos

The histone chaperone SET/TAF-Ibeta interacts functionally with the CREB-binding protein.

Zoe Karetsou1, Goran Martic, George Sflomos

  • 1Laboratory of Biological Chemistry, Medical School, University of Ioannina, 451 10 Ioannina, Greece.

Biochemical and Biophysical Research Communications
|August 3, 2005
PubMed
Summary

The oncoprotein SET/TAF-Ibeta, a histone chaperone, interacts with CREB-binding protein (CBP) to enhance gene transcription. This suggests a cooperative mechanism between histone chaperones and transcriptional regulators for gene activation.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Epigenetics

Background:

  • The oncoprotein SET/TAF-Ibeta functions as a histone chaperone involved in cell-cycle control and chromatin remodeling.
  • SET/TAF-Ibeta localizes to distinct foci within the nucleoplasm of interphase cells, visualized by confocal laser scanning microscopy.

Purpose of the Study:

  • To investigate the interaction between SET/TAF-Ibeta and CREB-binding protein (CBP).
  • To determine the effect of SET/TAF-Ibeta on the transcriptional activity of CBP.

Main Methods:

  • Confocal laser scanning microscopy to visualize SET/TAF-Ibeta localization.
  • Co-immunoprecipitation assays to confirm direct interaction between SET/TAF-Ibeta and CBP.
  • Reporter gene assays to assess the impact of SET/TAF-Ibeta on CBP-mediated transactivation.

Related Experiment Videos

Main Results:

  • SET/TAF-Ibeta directly interacts with the acetyltransferase CREB-binding protein (CBP).
  • SET/TAF-Ibeta enhances the transactivation potential of CBP.
  • The histone chaperone SET/TAF-Ibeta regulates CBP-mediated transcription.

Conclusions:

  • SET/TAF-Ibeta plays a role in regulating CBP-mediated transcription.
  • This interaction may represent a general mechanism for gene activation involving cooperation between transcriptional regulators and histone chaperones.