Abstract
A 22-kDa protein (P22), a direct counterpart to mammalian ornithine decarboxylase antizyme (ODC-AZ), was found in Selenomonas ruminantium, a gram-negative and anaerobic bacterium from sheep rumen. P22 does not degrade lysine/ornithine decarboxylase (LDC/ODC) but does bind to the AZ-binding region of LDC/ODC and triggers ATP-dependent proteolysis. This proteolytic system is totally compatible with the factors implicated in the AZ-mediated regulatory systems of mammalian ODC, such as mouse AZ or 26S proteasomes. Surprisingly, P22 is an L10 protein, a component of the large subunit of the bacterial ribosome. Interestingly, our research on bacterial antizyme was originally initiated from the study on the peptidoglycan of S. ruminantium, which contained covalently linked cadaverine, representing quite unusual characteristic among bacterial cell wall. In this chapter, we describe the chemical structure and biological function of the cadaverine-containing peptidoglycan of S. ruminantium, and the cellular biosynthesis of cadaverine by LDC/ODC and its P22 (=L10)-mediated regulation. In addition, we briefly refer to the phylogenetic distribution of LDC/ODC and ribosomal L10 among bacteria.
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Acknowledgments
We are grateful to all those who have supported us in our recovery and continued research following the crisis that occurred on 11 March 2011. We wish to express our sincere and heartfelt concern for the people still suffering as a result of the disaster, and wish them full and early recovery with fondest regards. We are also grateful to the director of the Center for Academic Publications Japan for permission to reproduce some sentences from the following paper: Journal of Nutritional Science and Vitaminology 58:153–156 (2012) by S. Kojima and Y. Kamio. Our works cited in this article were supported in part by Grants-in-Aid for Scientific Research from the Japan Society for the Promotion of Science.
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Kamio, Y., Yamaguchi, Y., Kaneko, J. (2015). Bacterial Antizyme. In: Kusano, T., Suzuki, H. (eds) Polyamines. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55212-3_8
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DOI: https://doi.org/10.1007/978-4-431-55212-3_8
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