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TATA binding protein associated factor 3 (TAF3) interacts with p53 and inhibits its function

Orsolya Bereczki1, Zsuzsanna Ujfaludi, Norbert Pardi

  • 1Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary. opszin@gmail.com

BMC Molecular Biology
|June 14, 2008
PubMed
Abstract

Insights

Researchers discovered TAF3, a protein interacting with p53, acts as a conserved negative regulator. This interaction impacts p53’s gene transcription and protein levels, offering insights into genome protection mechanisms.

Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • The tumor suppressor protein p53 regulates crucial cellular processes like genome protection and apoptosis by controlling gene expression.
  • Understanding the regulation of p53's transcription function is key to comprehending its multifaceted roles.

Purpose of the Study:

  • To investigate the regulatory mechanisms governing p53 transcription function.
  • To identify novel interacting partners of p53.

Main Methods:

  • Yeast two-hybrid assays to detect protein-protein interactions.
  • In vitro binding assays to confirm physical interactions.
  • Functional assays in human cell lines to assess the impact of TAF3 on p53 activity.

Main Results:

  • Identified BIP2 (Bric-à-brac interacting protein 2), the fly homolog of TAF3, as a binding partner of Drosophila melanogaster p53 (Dmp53).
  • Confirmed physical interaction between the C terminus of Dmp53 and the central region of TAF3.
  • Demonstrated that TAF3 interacts with both Dmp53 and human p53, indicating evolutionary conservation.
  • Showed that elevated TAF3 expression inhibits p53-mediated transcription activation and reduces p53 protein levels in human cells.

Conclusions:

  • TAF3 is identified as an evolutionarily conserved protein that negatively regulates the transcription activation function of p53.
  • This interaction between TAF3 and p53 has functional significance in controlling p53 activity and protein stability.

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