Abstract
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-kappaB (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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Binding, Competitive
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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Chromatography, Affinity
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Chromosomal Proteins, Non-Histone
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Conserved Sequence*
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Cross-Linking Reagents
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DNA-Binding Proteins
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Dimerization
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Dimethyl Suberimidate
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Glutathione Transferase / metabolism
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Intracellular Signaling Peptides and Proteins*
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Mice
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Multigene Family
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Nuclear Proteins / metabolism
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Peptides / metabolism
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Phosphoproteins / chemistry
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Phosphoproteins / metabolism*
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Protein Binding
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Protein Biosynthesis
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Recombinant Fusion Proteins / metabolism
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Sequence Deletion
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Tumor Suppressor p53-Binding Protein 1
Substances
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Carrier Proteins
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Chromosomal Proteins, Non-Histone
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Cross-Linking Reagents
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DNA-Binding Proteins
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Intracellular Signaling Peptides and Proteins
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Nuclear Proteins
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Peptides
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Phosphoproteins
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Recombinant Fusion Proteins
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Trp53bp1 protein, mouse
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Tumor Suppressor p53-Binding Protein 1
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Dimethyl Suberimidate
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Glutathione Transferase