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Mol Cell Biol, March 1998, p. 1477-1488, Vol. 18, No. 3
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

ETS-Mediated Cooperation between Basic Helix-Loop-Helix Motifs of the Immunoglobulin µ Heavy-Chain Gene Enhancer

Wei Dang,1 Xiao-hong Sun,2 and Ranjan Sen3,*

Rosenstiel Basic Medical Sciences Research Center3 and Departments of Biology and Biochemistry,1 Brandeis University, Waltham, Massachusetts 02254-9110, and Department of Cell Biology, New York University Medical Center, New York, New York 100162

Received 11 August 1997/Returned for modification 22 September 1997/Accepted 29 November 1997

The µE motifs of the immunoglobulin µ heavy-chain gene enhancer bind ubiquitously expressed proteins of the basic helix-loop-helix (bHLH) family. These elements work together with other, more tissue-restricted elements to produce B-cell-specific enhancer activity by presently undefined combinatorial mechanisms. We found that µE2 contributed to transcription activation in B cells only when the µE3 site was intact, providing the first evidence for functional interactions between bHLH proteins. In vitro assays showed that bHLH zipper proteins binding to µE3 enhanced Ets-1 binding to µA. One of the consequences of this protein-protein interaction was to facilitate binding of a second bHLH protein, E47, to the µE2 site, thereby generating a three-protein-DNA complex. Furthermore, transcriptional synergy between bHLH and bHLH zipper factors also required an intermediate ETS protein, which may bridge the transcription activation domains of the bHLH factors. Our observations define an unusual form of cooperation between bHLH and ETS proteins and suggest mechanisms by which tissue-restricted and ubiquitous factors combine to generate tissue-specific enhancer activity.

* Corresponding author. Mailing address: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South St., Waltham, MA 02254-9110. Phone: (781) 736-2455. Fax: (781) 736-2405. E-mail: sen{at}binah.cc.brandeis.edu.




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