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J. Biol. Chem., Vol. 281, Issue 7, 3995-4001, February 17, 2006

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Characterization of a Counterpart to Mammalian Ornithine Decarboxylase Antizyme in Prokaryotes^*

Yoshihiro Yamaguchi¹, Yumiko Takatsuka¹, Senya Matsufuji, Yasuko Murakami, and Yoshiyuki Kamio²

From the Laboratory of Applied Microbiology, Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumi-dori Amamiya-machi, Aoba-ku, Sendai 981-8555, and the Second Department of Biochemistry, Jikei University School of Medicine, Nishi-shinbashi, Minato-ku, Tokyo 105-8461, Japan

The degradation of mammalian ornithine decarboxylase (ODC) (EC 4.1.1.17 [EC] ) by 26 S proteasome, is accelerated by the ODC antizyme (AZ), a trigger protein involved in the specific degradation of eukaryotic ODC. In prokaryotes, AZ has not been found. Previously, we found that in Selenomonas ruminantium, a strictly anaerobic and Gram-negative bacterium, a drastic degradation of lysine decarboxylase (LDC; EC 4.1.1.18 [EC] ), which has decarboxylase activities toward both L-lysine and L-ornithine with similar K_m values, occurs upon entry into the stationary phase of cell growth by protease together with a protein of 22 kDa (P22). Here, we show that P22 is a direct counterpart of eukaryotic AZ by the following evidence. (i) P22 synthesis is induced by putrescine but not cadaverine. (ii) P22 enhances the degradation of both mouse ODC and S. ruminantium LDC by a 26 S proteasome. (iii) S. ruminantium LDC degradation is also enhanced by mouse AZ replacing P22 in a cell-free extract from S. ruminantium. (iv) Both P22 and mouse AZ bind to S. ruminantium LDC but not to the LDC mutated in its binding site for P22 and AZ. In this report, we also show that P22 is a ribosomal protein of S. ruminantium.

Received for publication, July 12, 2005 , and in revised form, December 8, 2005.

^* This work was supported in part by the Noda Institute for Scientific Research Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipient of a postdoctoral fellowship from Japan Society for the Promotion of Science.

² To whom correspondence should be addressed. Tel.: 81-22-717-8779; Fax: 81-22-717-8780; E-mail: ykamio{at}biochem.tohoku.ac.jp.

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				Y. Yamaguchi, Y. Takatsuka, and Y. Kamio Two Segments in Bacterial Antizyme P22 Are Essential for Binding and Enhance Degradation of Lysine/Ornithine Decarboxylase in Selenomonas ruminantium J. Bacteriol., January 1, 2008; 190(1): 442 - 446. [Abstract] [Full Text] [PDF]

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