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J. Biol. Chem., Vol. 276, Issue 39, 36849-36856, September 28, 2001
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From the The Maf oncoprotein is a basic leucine zipper
(bZip)-bearing transcriptional activator that recognizes the Maf
recognition element (MARE) DNA sequence. In this study, we investigated
the role of Maf's transactivation function in cell transformation. Replacement of the conserved amino terminus transactivator domain of
Maf by a heterologous and stronger transactivator domain (the acidic
transactivator domain of VP16) resulted in enhanced transformation of
chicken embryo fibroblast cells. In contrast, the fusing of a
transcriptional repressor domain (Sin3 interaction domain of Mxi1) with
the whole Maf protein masked the transactivator function of Maf, which
in turn inhibited its transforming activity. Furthermore, the leucine
zipper domain of Maf, which defines its dimer-forming specificity, was
exchangeable with that of GCN4 yeast protein in terms of its
transactivating and cell transforming activities. Thus, heterodimer
formation with other bZip factors is not required for Maf's ability to
transform. These results together suggest that transactivation through
MARE is necessary for Maf-induced transformation and that there exist
downstream target gene(s) for transformation. Since the MARE sequence
overlaps with the recognition element of another bZip oncoprotein Jun,
we assessed whether Jun and Maf induce cell transformation through
activating the same genes. We thus constructed a mutated version of Jun
that has a GCN4 leucine zipper and lacks the transactivator domain. This mutant repressed the cell transformation not only by Jun but also
by Maf. Thus, Maf and Jun share downstream target gene(s) that are
involved in cell transformation.
Maf and Jun Nuclear Oncoproteins Share Downstream Target Genes
for Inducing Cell Transformation*
§¶,§,,
Department of Virology, Institute of Medical
Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo
108-8639, § Frontier Collaborative Research Center, Tokyo
Institute of Technology, Yokohama 226-8503, Japan, and the
Department of Molecular and Experimental Medicine, Scripps
Research Institute, La Jolla, California 92037
*
This work was supported by a Grant-in-Aid for Scientific
Research on Priority Areas from the Ministry of Education, Science, Sports and Culture in Japan (to K. K.).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.
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