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J. Biol. Chem., Vol. 276, Issue 24, 21325-21330, June 15, 2001

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Transcriptional Activation by a Matrix Associating Region-binding Protein
CONTEXTUAL REQUIREMENTS FOR THE FUNCTION OF BRIGHT^*

Mark H. Kaplan^§, Rui-Ting Zong, Richard F. Herrscher, Richard H. Scheuermann^¶, and Philip W. Tucker

From the  Institute for Molecular and Cellular Biology, University of Texas at Austin, Austin, Texas 78712-1075 and the ^¶ Department of Pathology, University of Texas Southwestern Medical Center, Dallas, Texas 75235

Bright (B cell regulator of IgH transcription) is a B cell-specific, matrix associating region-binding protein that 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 high mobility group-like DNA binding characteristics. Similar to one group of high mobility group 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 Eµ matrix associating regions. 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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