Differential Protein Expression During Growth on Medium Versus Long-Chain Alkanes in the Obligate Marine Hydrocarbon-Degrading Bacterium Thalassolituus oleivorans MIL-1

The marine obligate hydrocarbonoclastic bacterium MIL-1 metabolizes a broad range of aliphatic hydrocarbons almost exclusively as carbon and energy sources. We used LC-MS/MS shotgun proteomics to identify proteins involved in aerobic alkane degradation during growth on medium- ( -C ) or long-chain (...

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Bibliographic Details
Published in:Frontiers in microbiology 2018-12, Vol.9, p.3130-3130
Main Authors: Gregson, Benjamin H, Metodieva, Gergana, Metodiev, Metodi V, Golyshin, Peter N, McKew, Boyd A
Format: Article
Language:English
Subjects:
alkane degradation
long-chain alkanes
medium-chain alkanes
Microbiology
oil pollution
subterminal oxidation
Thalassolituus oleivorans
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Summary:The marine obligate hydrocarbonoclastic bacterium MIL-1 metabolizes a broad range of aliphatic hydrocarbons almost exclusively as carbon and energy sources. We used LC-MS/MS shotgun proteomics to identify proteins involved in aerobic alkane degradation during growth on medium- ( -C ) or long-chain ( -C ) alkanes. During growth on -C , expresses an alkane monooxygenase system involved in terminal oxidation including two alkane 1-monooxygenases, a ferredoxin, a ferredoxin reductase and an aldehyde dehydrogenase. In contrast, during growth on long-chain alkanes ( -C ), may switch to a subterminal alkane oxidation pathway evidenced by significant upregulation of Baeyer-Villiger monooxygenase and an esterase, proteins catalyzing ketone and ester metabolism, respectively. The metabolite (primary alcohol) generated from terminal oxidation of an alkane was detected during growth on C but not on C also suggesting alternative metabolic pathways. Expression of both active and passive transport systems involved in uptake of long-chain alkanes was higher when compared to the non-hydrocarbon control, including a TonB-dependent receptor, a FadL homolog and a specialized porin. Also, an inner membrane transport protein involved in the export of an outer membrane protein was expressed. This study has demonstrated the substrate range of is larger than previously reported with growth from -C up to -C . It has also greatly enhanced our understanding of the fundamental physiology of , a key bacterium that plays a significant role in natural attenuation of marine oil pollution, by identifying key enzymes expressed during the catabolism of -alkanes.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2018.03130