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The Journal of Immunology, 2001, 167: 1522-1534.
Copyright © 2001 by The American Association of Immunologists

Differential Regulation of Mouse Germline Ig {gamma}1 and {epsilon} Promoters by IL-4 and CD401

Chun-sheng Mao and Janet Stavnezer2

Department of Molecular Genetics, Program in Immunology and Virology, University of Massachusetts Medical School, Worcester MA 01655

Before Ig class switching, RNA transcription through the specific S regions undergoing recombination is induced by cytokines and other activators that induce and direct switching. The resulting germline (GL) transcripts are essential for switch recombination. To understand the differential regulation of mouse IgG1 and IgE, we compared the promoters for GL {gamma}1 and {epsilon} transcripts. We addressed the question of why the promoter that regulates GL {epsilon} transcription is more responsive to IL-4 than the {gamma}1 promoter and also why GL {epsilon} transcription is more dependent on IL-4 than is {gamma}1 transcription. We found that the IL-4-responsive region of the GL {epsilon} promoter is more inducible than that of the {gamma}1 promoter, although each promoter contains a binding site for the IL-4-inducible transcription factor Stat6, located immediately adjacent to a binding site for a basic region leucine zipper (bZip) family protein. However, the arrangement and sequences of the sites differ between the {epsilon} and {gamma}1 promoters. The GL {epsilon} promoter binds Stat6 with a 10-fold higher affinity than does the {gamma}1 promoter. Furthermore, the bZip elements of the two promoters bind different transcription factors, as the GL {epsilon} promoter binds and is activated by AP-1, whereas the {gamma}1 promoter binds and is activated by activating transcription factor 2. C/EBP{beta} and C/EBP{gamma} also bind the {gamma}1 bZip element, although they inhibit rather than activate transcription. However, inhibition of promoter activity by C/EBP{beta} does not require the bZip element and may instead occur via inhibiting the activity of NF-{kappa}B.




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