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J Biol Chem, Vol. 273, Issue 32, 19955-19964, August 7, 1998

Transcription Factor ZBP-89 Regulates the Activity of the Ornithine Decarboxylase Promoter

G. Lynn LawDagger , Hideaki Itoh§, David J. Law, Gregory J. MizeDagger , Juanita L. Merchantparallel , and David R. MorrisDagger

From the Dagger  Department of Biochemistry, University of Washington, Seattle, Washington 98195, the § Department of Biochemistry, Akita University School of Medicine, Akita City 010, Japan, and the parallel  Departments of Internal Medicine and Physiology, University of Michigan and  Howard Hughes Medical Institute, Ann Arbor, Michigan 48109

Appropriate cellular levels of polyamines are required for cell growth and differentiation. Ornithine decarboxylase is a key regulatory enzyme in the biosynthesis of polyamines, and precise regulation of the expression of this enzyme is required, according to cellular growth state. A variety of mitogens increase the level of ornithine decarboxylase activity, and, in most cases, this elevation is due to increased levels of mRNA. A GC box in the proximal promoter of the ornithine decarboxylase gene is required for basal and induced transcriptional activity, and two proteins, Sp1 and NF-ODC1, bind to this region in a mutually exclusive manner. Using a yeast one-hybrid screening method, ZBP-89, a DNA-binding protein, was identified as a candidate for the protein responsible for NF-ODC1 binding activity. Three lines of evidence verified this identification; ZBP-89 copurified with NF-ODC1 binding activity, ZBP-89 antibodies specifically abolished NF-ODC1 binding to the GC box, and binding affinities of 12 different double-stranded oligonucleotides were indistinguishable between NF-ODC1, in nuclear extract, and in vitro translated ZBP-89. ZBP-89 inhibited the activation of the ornithine decarboxylase promoter by Sp1 in Schneider's Drosophila line 2, consistent with properties previously attributed to NF-ODC1.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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