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Molecular and Cellular Biology, April 1999, p. 2946-2957, Vol. 19, No. 4
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Transcriptional Activation by ETS and Leucine Zipper-Containing Basic Helix-Loop-Helix Proteins

Gang Tian,1 Batu Erman,1 Haruhiko Ishii,2 Samudra S. Gangopadhyay,1 and Ranjan Sen1,*

Rosenstiel Research Center, Department of Biology,1 and Biophysics Program,2 Brandeis University, Waltham, Massachusetts 02254

Received 2 November 1998/Returned for modification 13 November 1998/Accepted 18 January 1999

The immunoglobulin µ heavy-chain gene enhancer contains closely juxtaposed binding sites for ETS and leucine zipper-containing basic helix-loop-helix (bHLH-zip) proteins. To understand the µ enhancer function, we have investigated transcription activation by the combination of ETS and bHLH-zip proteins. The bHLH-zip protein TFE3, but not USF, cooperated with the ETS domain proteins PU.1 and Ets-1 to activate a tripartite domain of this enhancer. Deletion mutants were used to identify the domains of the proteins involved. Both TFE3 and USF enhanced Ets-1 DNA binding in vitro by relieving the influence of an autoinhibitory domain in Ets-1 by direct protein-protein associations. Several regions of Ets-1 were found to be necessary, whereas the bHLH-zip domain was sufficient for this effect. Our studies define novel interactions between ETS and bHLH-zip proteins that may regulate combinatorial transcription activation by these protein families.

* Corresponding author. Mailing address: Rosenstiel Research Center, Department of Biology, Brandeis University, Waltham, MA 02254. Phone: (781) 736-2400. Fax: (781) 736-2405. E-mail: sen{at}binah.cc.brandeis.edu.

Molecular and Cellular Biology, April 1999, p. 2946-2957, Vol. 19, No. 4
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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