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J Biol Chem, Vol. 275, Issue 1, 248-254, January 7, 2000

The Coiled Coil Dimerization Element of the Yeast Transcriptional Activator Hap1, a Gal4 Family Member, Is Dispensable for DNA Binding but Differentially Affects Transcriptional Activation*

Angela HachDagger , Thomas HonDagger , and Li Zhang§

From the Department of Biochemistry, New York University School of Medicine, New York, New York 10016

The heme activator protein Hap1 is a member of the yeast Gal4 family, which consists of transcription factors with a conserved Zn2Cys6 cluster that recognizes a CGG triplet. Many members of the Gal4 family contain a coiled coil dimerization element and bind symmetrically to DNA as homodimers. However, Hap1 possesses two unique properties. First, Hap1 binds asymmetrically to a direct repeat of two CGG triplets. Second, Hap1 binds to two classes of DNA elements, UAS1/CYC1 and UAS/CYC7, and permits differential transcriptional activation at these sites. Here we determined the residues of the Hap1 dimerization domain critical for DNA binding and differential transcriptional activation. We found that the Hap1 dimerization domain is composed of functionally redundant elements that can substitute each other in DNA binding and transcriptional activation. Remarkably, deletion of the coiled coil dimerization element did not severely diminish DNA binding and transcriptional activation at UAS1/CYC1 but completely abolished transcriptional activation at UAS/CYC7. Furthermore, Ala substitutions in the dimerization element selectively diminished transcriptional activation at UAS/CYC7. These results strongly suggest that the coiled coil dimerization element is responsible for differential transcriptional activation at UAS1/CYC1 and UAS/CYC7 and for making contacts with a putative coactivator or part of the transcription machinery.

* This work was supported by National Science Foundation Grant MCB-9617472 and National Institutes of Health Grant GM53453 (to L. Z.).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 These authors contributed to this work equally.

§ To whom correspondence should be addressed: Dept. of Biochemistry, NYU School of Medicine, 550 First Ave., New York, NY 10016. Tel.: 212-263-8506; Fax: 212-263-8166; E-mail: zhangl02@mcrcr0.med.nyu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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