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*
Department of Immunobiology and Cancer, Oklahoma Medical Research Foundation, and
Department of Microbiology and Immunology, Oklahoma University Health Sciences Center, Oklahoma City, OK 73104;
Department of Oral and Maxillo-Facial Surgery, Saga Medical School, Saga, Japan;
§
Department of Pediatrics, University of Tennessee, Memphis, TN 38105
Binding of the transcription factor Bright to Ig heavy chain loci after B cell activation is associated with increased heavy chain transcription. We now report that Bright coprecipitates with Bruton’s tyrosine kinase (Btk), the defective enzyme in X-linked immunodeficiency disease (xid). Furthermore, we observed Btk in the nucleus of activated murine B cells, and mobility shift assays suggest that it is a component of the Bright DNA-binding complex. While Bright protein was synthesized in activated spleen cells from xid mice, it did not bind DNA or associate stably with Btk. These data suggest that deficiencies in Bright DNA-binding activity may contribute to the defects in Ig production seen in xid mice.
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