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Originally published In Press as doi:10.1074/jbc.M105675200 on August 13, 2001

J. Biol. Chem., Vol. 276, Issue 44, 40537-40544, November 2, 2001
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The Basic Helix-Loop-Helix Domain of the Aryl Hydrocarbon Receptor Nuclear Transporter (ARNT) Can Oligomerize and Bind E-box DNA Specifically*

Joy L. HuffmanDagger §, Asawari MokashiDagger §||, Hans Peter BächingerDagger ||**, and Richard G. BrennanDagger Dagger Dagger

From the Dagger  Department of Biochemistry and Molecular Biology, Oregon Health Sciences University and || Portland Shriners Hospital, Portland, Oregon 97201

The aryl hydrocarbon receptor nuclear transporter (ARNT) is a basic helix-loop-helix (bHLH) protein that contains a Per-Arnt-Sim (PAS) domain. ARNT heterodimerizes in vivo with other bHLH PAS proteins to regulate a number of cellular activities, but a physiological role for ARNT homodimers has not yet been established. Moreover, no rigorous studies have been done to characterize the biochemical properties of the bHLH domain of ARNT that would address this issue. To begin this characterization, we chemically synthesized a 56-residue peptide encompassing the bHLH domain of ARNT (residues 90-145). In the absence of DNA, the ARNT-bHLH peptide can form homodimers in lower ionic strength, as evidenced by dynamic light scattering analysis, and can bind E-box DNA (CACGTG) with high specificity and affinity, as determined by fluorescence anisotropy. Dimers and tetramers of ARNT-bHLH are observed bound to DNA in equilibrium sedimentation and dynamic light scattering experiments. The homodimeric peptide also undergoes a coil-to-helix transition upon E-box DNA binding. Peptide oligomerization and DNA affinity are strongly influenced by ionic strength. These biochemical and biophysical studies on the ARNT-bHLH reveal its inherent ability to form homodimers at concentrations supporting a physiological function and underscore the significant biochemical differences among the bHLH superfamily.

* 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.

§ These authors contributed equally to this work.

Supported by a National Institutes of Health predoctoral training grant and a Tartar Trust Foundation grant.

** Supported by a Shriners Hospital grant.

Dagger Dagger Supported by National Institutes of Health Grant GM-49244. To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Oregon Health Sciences University, 3181 S. W. Sam Jackson Park Rd., Portland, OR 97201. Tel.: 503-494-4427; Fax: 503-494-8393; E-mail: brennanr@ohsu.edu.

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


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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.