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</script>The high mobility group protein HMG I(Y) stimulates the binding of a specific isoform of the activating transcription factor 2 (ATF-2(195)) to the interferon beta (IFN-beta) gene promoter. HMG I(Y) specifically interacts with the basic-leucine zipper region of ATF-2(195), and HMG I(Y) binds to two sites immediately flanking the ATF-2 binding site of the IFN-beta promoter. Here, we show that HMG I(Y) can stimulate the binding of ATF-2(195), at least in part, by promoting ATF-2 dimerization. In addition, we report the characterization of a naturally occurring isoform of ATF-2 (ATF-2(192)) that binds specifically to the IFN-beta promoter but is unable to interact with HMG I(Y). Remarkably, HMG I(Y) inhibits the binding of ATF-2(192) to the IFN-beta promoter. Thus, the ability of HMG I(Y) to specifically interact with ATF-2 correlates with its ability to stimulate ATF-2 binding to the IFN-beta promoter. Comparisons of the amino acid sequences of the basic-leucine zipper domains of ATF-2(195) and ATF-2(192) suggest that HMG I(Y) interacts with a short stretch of basic amino acids near the amino terminus of the basic-leucine zipper domain of ATF-2(195).
Leucine Zippers, Activating Transcription Factor 2, Macromolecular Substances, Molecular Sequence Data, High Mobility Group Proteins, NF-kappa B, Zinc Fingers, DNA, Interferon-beta, In Vitro Techniques, Regulatory Sequences, Nucleic Acid, Recombinant Proteins, DNA-Binding Proteins, Mice, Animals, Amino Acid Sequence, HMGA1a Protein, Cloning, Molecular, Cyclic AMP Response Element-Binding Protein, Transcription Factors
Leucine Zippers, Activating Transcription Factor 2, Macromolecular Substances, Molecular Sequence Data, High Mobility Group Proteins, NF-kappa B, Zinc Fingers, DNA, Interferon-beta, In Vitro Techniques, Regulatory Sequences, Nucleic Acid, Recombinant Proteins, DNA-Binding Proteins, Mice, Animals, Amino Acid Sequence, HMGA1a Protein, Cloning, Molecular, Cyclic AMP Response Element-Binding Protein, Transcription Factors
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