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Stimulation of Cytoplasmic DNA Sensing Pathways In Vitro and In Vivo
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The interferon-inducible growth-inhibitory p202 protein: DNA binding properties and identification of a DNA binding

D Choubey1, J U Gutterman

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

Biochemical and Biophysical Research Communications
|April 16, 1996
PubMed

Insights

The interferon-inducible protein p202 binds to DNA, both double- and single-stranded. This DNA binding ability, intrinsic to p202, may contribute to its cell proliferation inhibition functions.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Virology

Background:

  • p202 is an interferon-inducible protein.
  • p202 expression inhibits cell proliferation.
  • p202 interacts with retinoblastoma protein and transcription factors (AP-1, NF-kappaB).

Purpose of the Study:

  • To investigate the DNA-binding properties of p202.
  • To determine if DNA binding is an intrinsic function of p202.
  • To identify regions of p202 involved in DNA binding.

Main Methods:

  • In vitro DNA binding assays using recombinant p202.
  • Analysis of a C-terminal deletion mutant of p202.
  • Assessment of DNA binding in relation to protein phosphorylation.

Main Results:

  • p202 binds nonspecifically to both double-stranded and single-stranded DNA.
  • DNA binding activity is intrinsic to p202 and independent of its C-terminus.
  • Underphosphorylated p202 demonstrates efficient DNA binding.

Conclusions:

  • The intrinsic DNA binding capability of p202 is a key feature.
  • The C-terminus of p202 is not essential for its DNA binding function.
  • p202's DNA binding likely contributes to its antiproliferative effects.

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