2013 Fiscal Year Final Research Report
Molecular basis for the maintenance of envelope integrity in Selenomonas ruminantium: Controlled mechanism of cadaverine biosynthesis which covalently links to the peptidoglycan
| Project/Area Number |
23380046
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Shokei Gakuin College (2013)
Tohoku University (2012)
Yamagata University (2011) |
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Principal Investigator |
KAMIO Yoshiyuki 尚絅学院大学, 総合人間科学部, 名誉教授 (00109175)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Isao 北海道大学, 大学院・先端科学研究科, 特任教授 (70093052)
KANEKO Jun 東北大学, 大学院・農学研究科, 准教授 (30221188)
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| Co-Investigator(Renkei-kenkyūsha) |
TAKATSUKA Yumiko 山形大学, 大学院・理工学研究科, 助教 (70570810)
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| Project Period (FY) |
2011-04-01 – 2014-03-31
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| Keywords | バクテリアアンチザイム / リボソーム蛋白質L-10 / L10遺伝子 / ポリアミン生合成制御機構 / ペプチドグリカン結合型ポリアミン / ClpXP protease |
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| Research Abstract |
Selenomonas ruminantium has cadaverine(Cad),which links covalently to the peptidoglycan (PG) for the cell devision.In this bacterium,Cad is synthesized constitutively from L-lysine by lysine/ornithine decarboxylase (LDC/ODC) and transferred to PG. Here,we found that (1) LDC/ODC was degraded at an early stationary phase by ATP dependent ClpXP.This degradation requires a ribosomal protein L10 which is induced into cytoplasm by putrescine in the cells. The induced L10 has similar biochemical and biophysical characteristics to those of an antizyme (AZ),which have been reported only in mammalian cells.(2) PG-bound Cad mediates an interaction between PG and the periplasm-exposed S-layer homologous domain of Mep45, a major outer membrane (OM) protein of this bacterium, thereby forms the structural linkage between the PG and OM.(3)The gene of lipid intermediate:diamine transferase (Ldt) for cadaverine-adding reaction into the lipid intermediate was cloned and the gene product was purified.
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