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J. Biol. Chem., Vol. 276, Issue 24, 21325-21330, June 15, 2001
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§,,,
From the 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.
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
To whom correspondence should be addressed: Inst. for
Molecular and Cellular Biology, University of Texas at Austin, 100 W 24th St., ESB-534, Austin, TX 78712-1095. Tel.: 512-475-7705; Fax:
512-475-7707; E-mail: philtucker@mail.utexas.edu.
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