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p202 self-associates through a sequence conserved among the members of the 200-family proteins

D Koul1, N U Obeyesekere, J U Gutterman

  • 1Department of Molecular Oncology, The University of Texas M.D. Anderson Cancer Center, Houston 77030, USA.

FEBS Letters
|November 20, 1998
PubMed

Insights

Murine p202, an interferon-inducible protein, inhibits cell colony formation. This study shows p202 self-associates, suggesting a novel regulatory mechanism for its activity.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Murine p202 is an interferon-inducible nuclear phosphoprotein.
  • p202 (52 kDa) inhibits colony formation in transfected cells.
  • It interacts with key cellular proteins including pocket proteins, p53-binding protein, and transcription factors.

Purpose of the Study:

  • To investigate the self-association properties of murine p202.
  • To identify the region responsible for p202 self-association.
  • To explore the implications of self-association on p202 activity regulation.

Main Methods:

  • Transfection of cells with p202.
  • In vitro assays to demonstrate direct self-association.
  • Analysis of conserved sequences within the p202 protein family.

Main Results:

  • Murine p202 directly self-associates.
  • A conserved sequence within p202 is sufficient for this self-association in vitro.
  • p202 modulates the transcriptional activity of various factors it binds.

Conclusions:

  • p202 self-association is a direct interaction.
  • This self-association may serve as a regulatory mechanism for p202 function.
  • Understanding p202 self-association provides insights into interferon-inducible gene regulation.

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