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Structural insights into interactions of C/EBP transcriptional activators with the Taz2 domain of p300

Prasenjit Bhaumik1, Jamaine Davis1, Joseph E Tropea2

  • 1Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA.

Acta Crystallographica. Section D, Biological Crystallography
|July 10, 2014
PubMed

Insights

Transcription factors C/EBP bind to p300/CBP

Area of Science:

  • Molecular Biology
  • Protein-protein interactions
  • Transcription regulation

Background:

  • C/EBP transcription factors regulate gene expression.
  • p300/CBP proteins are crucial coactivators involved in transcription.
  • C/EBP proteins interact with p300/CBP, mediating phosphorylation via kinase recruitment.

Purpose of the Study:

  • To elucidate the structural basis of C/EBP transcription factor interaction with the p300/CBP Taz2 domain.
  • To understand how conserved homology boxes in C/EBP mediate specific binding to p300/CBP.
  • To investigate the implications of this interaction for C/EBP-mediated transcriptional regulation.

Main Methods:

  • X-ray crystallography of a chimeric protein (p300 Taz2 and C/EBPℇ).
  • Structural analysis of protein-protein interactions.
  • Bioinformatic analysis of conserved motifs and domains.

Main Results:

  • The crystal structure revealed that the C/EBPℇ transactivation domain (TAD) forms two helices that interact with the p300 Taz2 domain.
  • This interaction involves a symmetry-related Taz2 molecule, suggesting a specific binding mode.
  • The N-termini of C/EBP proteins are likely unbound, consistent with HIPK2 kinase docking.

Conclusions:

  • The C/EBP TAD interacts with the p300 Taz2 domain via a conserved helical structure.
  • This interaction mode is proposed to be conserved across the C/EBP family.
  • The findings provide insights into the assembly of transcription factor complexes and regulation by p300/CBP.
Keywords:
HIPK2ligand bindingmolecular recognitiontranscription

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