Characterization of a Counterpart to Mammalian Ornithine Decarboxylase Antizyme in Prokaryotes

• Published in: The Journal of biological chemistry Vol. 281; no. 7; pp. 3995 - 4001
• Main Authors: Yamaguchi, Yoshihiro, Takatsuka, Yumiko, Matsufuji, Senya, Murakami, Yasuko, Kamio, Yoshiyuki
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17.02.2006; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Animals; Bacterial Proteins - physiology; Base Sequence; Binding Sites; Carboxy-Lyases - metabolism; Mice; Molecular Sequence Data; Ornithine Decarboxylase - metabolism; Proteasome Endopeptidase Complex - physiology; Proteins - chemistry; Proteins - genetics; Proteins - physiology; Ribosomal Protein L10; Ribosomal Proteins - chemistry; Selenomonas - chemistry; Selenomonas - growth & development; Selenomonas ruminantium
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M507545200

The degradation of mammalian ornithine decarboxylase (ODC) (EC 4.1.1.17) 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), which has decarboxylase activities toward both l-lysine and l-ornithine with similar Km 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.