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Originally published In Press as doi:10.1074/jbc.M010658200 on March 19, 2001

J. Biol. Chem., Vol. 276, Issue 23, 19897-19904, June 8, 2001
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Independent Repression of a GC-rich Housekeeping Gene by Sp1 and MAZ Involves the Same cis-Elements*

Jun SongDagger §, Hideyo UgaiDagger , Ichiro Kanazawa§, Kailai Sun, and Kazunari K. YokoyamaDagger ||

From Dagger  RIKEN (The Insitute of Physical & Chemical Research), Tsukuba Institute, 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan, the § Department of Neurology, Institute of Brain Research, Faculty of Medicine, University of Tokyo, Tokyo 113-0033, Japan, and the  Department of Medical Genetics, China Medical University, Shenyang 110001, China

The transcription factors Sp1 and MAZ (Myc-associated zinc finger protein) contain several zinc finger motifs, and each functions as both a positive and a negative regulator of gene expression. In this study, we characterized the extremely GC-rich promoter of the human gene for MAZ, which is known as a housekeeping gene. Unique symmetrical motifs in the promoter region (nucleotides -383 to -334) were essential for the expression of the gene for MAZ, whereas an upstream silencer element (nucleotides -784 to -612) was found to act in a position-dependent but orientation-independent manner. Sp1 and MAZ bound to the same cis-elements in the GC-rich promoter, apparently sharing DNA-binding sites. The relative extent of binding of Sp1 and MAZ to these cis-elements corresponded to the extent of negative regulation of the expression of the gene for MAZ in various lines of cells. Furthermore, novel repressive domains in both Sp1 (amino acids 622-788) and MAZ (amino acids 127-292) were identified. Suppression by Sp1 and suppression by MAZ were independent phenomena; histone deacetylases were involved in the autorepression by MAZ itself, whereas DNA methyltransferase 1 was associated with suppression by Sp1. Our results indicate that both deacetylation and methylation might be involved in the regulation of expression of a single gene via the actions of different zinc finger proteins that bind to the same cis-elements.

* This work was supported by grants from the Special Coordination Funds of the Science and Technology Agency of Japan, the Life Science Projects of RIKEN, and the Ministry of Education, Science, Sports, and Culture of Japan (to K. K. Y.).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. Tel.: 81-298-36-3612; Fax: 81-298-36-9120; E-mail: yokoyama@rtc.riken.go.jp.

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