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Originally published In Press as doi:10.1074/jbc.M100080200 on March 15, 2001

J. Biol. Chem., Vol. 276, Issue 22, 18710-18716, June 1, 2001
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Conserved Regions of the Drosophila Erect Wing Protein Contribute Both Positively and Negatively to Transcriptional Activity*

Irina Kotovsky Fazio, Timothy A. BolgerDagger , and Grace Gill§

From the Department of Pathology, Harvard Medical School, Boston, Massachussetts 02115

Genetic studies of the Drosophila erect wing (ewg) gene have revealed that ewg has an essential function in the embryonic nervous system and is required for the specification of certain muscle cells. We have found that EWG is a site-specific transcriptional activator, and we report here that evolutionarily conserved regions of EWG contribute both positively and negatively to transcriptional activity. Using gel mobility shift assays, we have shown that an EWG dimer binds specifically to DNA. In transfection assays, EWG activated expression of a reporter gene bearing specific binding sites. Analysis of deletion mutants and fusions of EWG to the Gal4 DNA binding domain has identified a transcriptional activation domain in the C terminus of EWG. Deletion analysis also revealed a novel inhibitory region in the N terminus of EWG. Strikingly, both the activation domain and the inhibitory region are conserved in EWG homologs including human nuclear respiratory factor 1 (NRF-1) and the sea urchin P3A2 protein. The strong conservation of elements that determine transcriptional activity suggests that the EWG, NRF-1, and P3A2 family of proteins shares common mechanisms of action and has maintained common functions across evolution.

* This work was supported in part by March of Dimes Birth Defects Foundation Basil O'Connor Starter Scholar Research Award Grant 5-FY98-0555 (to G. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Cell and Molecular Biology Program, Duke University, Durham, NC 27710.

§ To whom correspondence should be addressed: Dept. of Pathology, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Tel.: 617-432-0985; Fax: 617-432-1313; E-mail: grace_gill@hms.harvard.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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