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Alkane inducible proteins in Geobacillus thermoleovorans B23

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タイトル: Alkane inducible proteins in Geobacillus thermoleovorans B23
著者: Kato, Tomohisa 著作を一覧する
Miyanaga, Asuka 著作を一覧する
Kanaya, Shigenori 著作を一覧する
Morikawa, Masaaki 著作を一覧する
発行日: 2009年 3月25日
出版者: BioMed Central Ltd.
誌名: BMC Microbiology
巻: 9
開始ページ: 60
出版社 DOI: 10.1186/1471-2180-9-60
抄録: Background: Initial step of β-oxidation is catalyzed by acyl-CoA dehydrogenase in prokaryotes and mitochondria, while acyl-CoA oxidase primarily functions in the peroxisomes of eukaryotes. Oxidase reaction accompanies emission of toxic by-product reactive oxygen molecules including superoxide anion, and superoxide dismutase and catalase activities are essential to detoxify them in the peroxisomes. Although there is an argument about whether primitive life was born and evolved under high temperature conditions, thermophilic archaea apparently share living systems with both bacteria and eukaryotes. We hypothesized that alkane degradation pathways in thermophilic microorganisms could be premature and useful to understand their evolution. Results: An extremely thermophilic and alkane degrading Geobacillus thermoleovorans B23 was previously isolated from a deep subsurface oil reservoir in Japan. In the present study, we identified novel membrane proteins (P16, P21) and superoxide dismutase (P24) whose production levels were significantly increased upon alkane degradation. Unlike other bacteria acyl-CoA oxidase and catalase activities were also increased in strain B23 by addition of alkane. Conclusion: We first suggested that peroxisomal β-oxidation system exists in bacteria. This eukaryotic-type alkane degradation pathway in thermophilic bacterial cells might be a vestige of primitive living cell systems that had evolved into eukaryotes.
資料タイプ: article
URI: http://hdl.handle.net/2115/38519
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

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