The interferon-inducible growth-inhibitory p202 protein: DNA binding properties and identification of a DNA binding domain.
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.
Choubey
D
D
Department of Molecular Oncology, University of Texas M.D. Anderson Cancer Center, Houston, 77030, USA.
Gutterman
J U
JU
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis* / Q000378:metabolism; D002460:Cell Line; D004268:DNA-Binding Proteins / Q000096:biosynthesis* / Q000378:metabolism; D007372:Interferons / Q000502:physiology*; D047908:Intracellular Signaling Peptides and Proteins; D051379:Mice; D010750:Phosphoproteins / Q000096:biosynthesis* / Q000378:metabolism; D010766:Phosphorylation
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; C092537:Ifi202b protein, mouse; D047908:Intracellular Signaling Peptides and Proteins; D010750:Phosphoproteins; D007372:Interferons