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

• Published in: FEBS letters Vol. 438; no. 1; pp. 21 - 24
• Main Authors: Koul, Dimpy, Obeyesekere, Nihal U, Gutterman, Jordan U, Mills, Gordon B, Choubey, Divaker
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 30-10-1998
• Subjects: 200-family proteins; Amino Acid Sequence; Animals; Binding Sites; Binding, Competitive; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Chromatography, Affinity; Chromosomal Proteins, Non-Histone; Conserved Sequence; Cross-Linking Reagents; Dimerization; Dimethyl Suberimidate; DNA-Binding Proteins; Glutathione Transferase - metabolism; Intracellular Signaling Peptides and Proteins; Mice; Multigene Family; Nuclear Proteins - metabolism; p202; Peptides - metabolism; Phosphoproteins - chemistry; Phosphoproteins - metabolism; Protein Binding; Protein Biosynthesis; Protein-protein interaction motif; Recombinant Fusion Proteins - metabolism; Self-association; Sequence Deletion; Tumor Suppressor p53-Binding Protein 1; 200-family proteins; Conserved sequence; Self-association; Protein-protein interaction motif; p202
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(98)01263-0

Murine p202 is an interferon-inducible primarily nuclear phosphoprotein (52 kDa) whose expression in transfected cells inhibits colony formation. p202-binding proteins include the pocket proteins (pRb, p107 and p130), a p53-binding protein (sm53BP1), and transcription factors (e.g. NF-κB (p50 and p65), AP-1 (c-Fos and c-Jun), E2F-1, E2F-4, MyoD, and myogenin). p202 modulates the transcriptional activity of these factors in transfected cells. Here we demonstrate that p202 self-associates directly and a sequence in p202, which is conserved among the members of the 200-family proteins, was sufficient for self-association in vitro. Our observations reported herein raise the possibility that self-association of p202 may provide a mechanism for the regulation of its activity.