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, Philip W. Tucker

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)21325-21330
Number of pages6
JournalJournal of Biological Chemistry
Volume276
Issue number24
DOIs
StatePublished - Jun 15 2001

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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