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Originally published In Press as doi:10.1074/jbc.M200283200 on January 25, 2002

J. Biol. Chem., Vol. 277, Issue 15, 12604-12612, April 12, 2002
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The Basic Helix-Loop-Helix Factor, HAND2, Functions as a Transcriptional Activator by Binding to E-boxes as a Heterodimer*

Yan-Shan DaiDagger § and Peter CserjesiDagger ||**

From the Dagger  Department of Anatomy and Cell Biology, Columbia University, New York, New York 10032 and the  Department of Cell Biology and Anatomy and the || Molecular and Human Genetics Center, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112

HAND2 (dHAND) is a basic helix-loop-helix (bHLH) transcription factor expressed in numerous tissues during development including the heart, limbs, and a subset of neural crest derivatives. Functional analysis has shown that HAND2 is involved in development of the branchial arches, heart, limb, vasculature, and nervous system. Although it is essential for development of numerous tissues, little is known about its mode of action. To this end, we have characterized HAND2 transcriptional regulatory mechanisms. Using mammalian one-hybrid analysis we show that HAND2 contains a strong transcriptional activation domain in the amino-terminal third of the protein. Like most tissue-restricted bHLH factors, HAND2 heterodimerizes with the broadly expressed bHLH factors, the E-proteins. We determined the consensus DNA binding site of HAND2 and show that HAND2 binds a subset of E-boxes as a heterodimer with E12. Yeast two-hybrid screening of a neuroblastoma cDNA library for HAND2-interacting proteins selected HAND2 and numerous additional members of the E-protein family. Although HAND2 homodimer formation was confirmed by in vitro analysis, HAND2 fails to homodimerize in a mammalian two-hybrid assay but demonstrates robust HAND2/E12 interaction. We conclude that HAND2 functions as a transcription activator by binding a subset of E-boxes as a heterodimer with E-proteins.

* This work was supported by grants from American Cancer Society, American Heart Association, March of Dimes Foundation, and Whitehall Foundation (to P. C.).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.

§ Present address: Division of Molecular Cardiovascular Biology Children's Hospital Research Foundation, Cincinnati, OH 45229.

** A Tobacco Research Scholar during part of this work. To whom correspondence should be addressed: Dept. of Cell Biology and Anatomy, Louisiana State University Health Sciences Center, 1901 Perdido St., New Orleans, LA 70112. Tel/Fax: 504-568-4018; E-mail: pcserj@lsuhsc.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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