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Originally published In Press as doi:10.1074/jbc.M110400200 on May 2, 2002

J. Biol. Chem., Vol. 277, Issue 28, 25115-25124, July 12, 2002
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The C-terminal Extension (CTE) of the Nuclear Hormone Receptor DNA Binding Domain Determines Interactions and Functional Response to the HMGB-1/-2 Co-regulatory Proteins*

Vida Senkus MelvinDagger , Sarah C. RoemerDagger , Mair E. A. ChurchillDagger §, and Dean P. EdwardsDagger ||

From the Dagger  Program in Molecular Biology and the Departments of § Pharmacology and  Pathology, University of Colorado Health Sciences Center, Denver, Colorado 80262

Previously, we and others reported that the high mobility group proteins, HMGB-1/-2, enhance DNA binding in vitro and transactivation in situ by the steroid hormone subgroup of nuclear receptors but did not influence these functions of class II receptors. We show here that the DNA binding domain (DBD) is sufficient to account for the selective influence of HMGB-1/-2 on the steroid class of receptors. Furthermore, the use of chimeric DBDs reveals that this selectivity is dependent on the C-terminal extension (CTE), amino acid sequences adjacent to the zinc finger core DBD. HMGB-1/-2 interact directly with the DBDs of steroid but not class II receptors, and this interaction requires the CTE. This in vitro interaction correlates with a requirement of the CTE for maximal HMGB-1/-2 enhancement of DNA binding in vitro and transcriptional activation in cells. Finally, class II receptor DBDs have a much higher intrinsic affinity for DNA than steroid receptor DBDs, and this affinity difference is also dependent on the CTE. These results reveal the importance of the steroid receptor CTE for DNA binding affinity and functional response to HMGB-1/-2.

* This work was supported by National Institutes of Health Grant RO1 CA46938 (to D. P. E.).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.

|| To whom correspondence should be addressed: Dept. of Pathology, University of Colorado Health Sciences Center, 4200 E. Ninth Ave., B216, Denver, CO 80262. Tel.: 303-315-5416; Fax: 303-315-6721; E-mail: dean.edwards@uchsc.edu.

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