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Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by

Sarah Burge1, Daniel P Teufel, Fiona M Townsley

  • 1Medical Research Council Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|February 17, 2009
PubMed

Insights

The p73 protein

Area of Science:

  • Molecular biology
  • Protein-protein interactions
  • Gene regulation

Background:

  • The p73 protein is a member of the p53 family, sharing functional similarities with p53.
  • p73 plays a role in transactivating target genes.

Purpose of the Study:

  • To characterize the interaction between the p73 N-terminus and domains of p300 and Mdm2.
  • To investigate the role of specific p73 N-terminal subdomains in transcriptional activity.

Main Methods:

  • Biophysical measurements
  • Cellular assays
  • Mutant analysis (QS, T14A, T14D)

Main Results:

  • p73 N-terminus has two transactivation subdomains (residues 10-30 and 46-67).
  • p73 N-terminus binds p300 domains with varying affinities, notably submicromolar for Taz2.
  • Phosphorylation at T14 enhances p73 N-terminus affinity for Taz2 and increases transactivation.

Conclusions:

  • The p73 N-terminus interaction with p300 is crucial for its transactivation function.
  • Phosphorylation of p73 at T14 significantly modulates its interaction with p300 and transcriptional activity.

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