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Papers In Press, published online ahead of print April 6, 2001
J. Biol. Chem, 10.1074/jbc.M100836200
Submitted on January 29, 2001
Revised on March 30, 2001
Accepted on April 5, 2001
Molecular Genetics & Microbiology, University of Texas at Austin, Austin, TX 78705
Corresponding Author: philtucker{at}mail.utexas.edu
SUMMARY Bright (B cell regulator of IgH transcription) is a B cell-specific, MAR binding protein which transactivates gene expression from the IgH intronic enhancer (Eµ). We show here that Bright has multiple contextual requirements to function as a transcriptional activator. Bright cannot transactivate via out-of-context, concatenated binding sites. Transactivation is maximal on integrated substrates. Two of the three previously identified binding sites in Eµ are required for full Bright transactivation. The Bright DNA binding domain defined a new family which includes Swi1, a component of the Swi/Snf complex shown to have HMG-like DNA binding characteristics. Similar to one group of HMG box proteins, Bright distorts Eµ binding site-containing DNA on binding, supporting the concept that it mediates Eµ remodeling. Transfection studies further implicate Bright in facilitating spatially separated promoter-enhancer interactions in both transient and stable assays. Finally, we show that overexpression of Bright leads to enhanced DNase I sensitivity of the endogenous Em MARs. These data further suggest that Bright may contribute to increased gene expression by remodeling the immunoglobulin locus during B cell development.
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