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Originally published In Press as doi:10.1074/jbc.M103426200 on May 16, 2001

J. Biol. Chem., Vol. 276, Issue 29, 27657-27662, July 20, 2001
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A Novel Ikappa B Protein, Ikappa B-zeta , Induced by Proinflammatory Stimuli, Negatively Regulates Nuclear Factor-kappa B in the Nuclei*

Soh Yamazaki, Tatsushi MutaDagger , and Koichiro Takeshige

From the Department of Molecular and Cellular Biochemistry, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan

The transcription factor nuclear factor-kappa B (NF-kappa B) plays crucial roles in a wide variety of cellular functions and its activity is strictly regulated by cytosolic inhibitors known as Ikappa Bs. We here report a new member of the Ikappa B protein family, Ikappa B-zeta , harboring six ankyrin repeats at its carboxyl terminus. Ikappa B-zeta mRNA is strongly induced after stimulation by lipopolysaccharide. The induction of Ikappa B-zeta is also observed by stimulation with interleukin-1beta but not by tumor necrosis factor-alpha . In contrast to cytosolic Ikappa B-alpha , -beta , and -epsilon , the induced Ikappa B-zeta localizes in the nucleus via its amino-terminal region, which shows no homology with other proteins. Transiently expressed Ikappa B-zeta inhibits the NF-kappa B activity without affecting the nuclear translocation of NF-kappa B upon stimulation. The expressed Ikappa B-zeta preferentially associates with the NF-kappa B subunit p50 rather than p65 and recombinant Ikappa B-zeta proteins inhibit the DNA binding of the p65/p50 heterodimer and the p50/p50 homodimer. Thus, Ikappa B-zeta negatively regulates NF-kappa B activity in the nucleus, possibly in order to prevent excessive inflammation. Moreover, transfection of Ikappa B-zeta renders cells more susceptible to apoptosis induced by tumor necrosis factor-alpha . The proapoptotic activity of Ikappa B-zeta further suggests that it might be one of key regulators for inflammation and other biologically relevant processes.

* This work was supported in part by grants-in-aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan (to T. M. and K. T.), and grants from the Mochida Memorial Foundation for Medical and Pharmaceutical Research (to T. M.), Sumitomo Foundation (to T. M.), and Kaibara Foundation (to T. M.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with acession number(s) AB047549.

Dagger To whom correspondence should be addressed: Dept. of Molecular and Cellular Biochemistry, Graduate School of Medical Sciences, Kyushu University, 3-1-1, Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. Tel./Fax: 81-92-642-6103; E-mail: tmuta@mailserver.med.kyushu-u.ac.jp.

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