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  • Title: The interferon-inducible growth-inhibitory p202 protein: DNA binding properties and identification of a DNA binding domain.
    Author: Choubey D, Gutterman JU.
    Journal: Biochem Biophys Res Commun; 1996 Apr 16; 221(2):396-401. PubMed ID: 8619867.
    Abstract:
    p202 is an interferon-inducible protein whose expression in transfected cells inhibits proliferation. p202 binds to the retinoblastoma tumor suppressor protein in vitro and in vivo and the transcription factors AP-1 c-Fos and c-Jun, NF-kappaB p50 and p65, and inhibits the transcriptional activity of these factors in vivo. Here we report that p202 nonspecifically binds to double-stranded DNA and to single-stranded DNA in vitro. Analysis with recombinant p202 revealed that DNA binding activity is intrinsic to p202. A C-terminal deletion mutant of p202 exhibited DNA-binding properties, indicating that the C-terminus is dispensable for DNA binding. We also found that underphosphorylated p202 efficiently binds to DNA. Our data suggest that DNA binding activity of p202 may contribute to its functions.
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