Alkane inducible proteins in Geobacillus thermoleovorans B23Report as inadecuate




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BMC Microbiology

, 9:60

First Online: 25 March 2009Received: 09 September 2008Accepted: 25 March 2009

Abstract

BackgroundInitial 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.

ResultsAn 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.

ConclusionWe 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.

Abbreviationsbpbase pairs

kbkilobase pairs.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2180-9-60 contains supplementary material, which is available to authorized users.

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Author: Tomohisa Kato - Asuka Miyanaga - Shigenori Kanaya - Masaaki Morikawa

Source: https://link.springer.com/article/10.1186/1471-2180-9-60







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