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Anaerobic degradation of 4-methylbenzoate via a specific 4-methylbenzoyl-CoA pathway

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Lahme,  S.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Kube,  M.
Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Wilkes,  H.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Reinhardt,  R.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Rabus,  R.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Citation

Lahme, S., Eberlein, C., Jarling, R., Kube, M., Boll, M., Wilkes, H., et al. (2012). Anaerobic degradation of 4-methylbenzoate via a specific 4-methylbenzoyl-CoA pathway. Environmental Microbiology, 14(5), 1118-1132.


Cite as: http://hdl.handle.net/21.11116/0000-0001-C835-2
Abstract
The pathway for anaerobic degradation of 4-methylbenzoate was studied in the denitrifying alphaproteobacterium Magnetospirillum sp. strain pMbN1. Adaptation studies with whole cells indicated substrate-dependent induction of the capacity to degrade 4-methylbenzoate. Differential protein profiling (2D-DIGE) of 4-methylbenzoate- in comparison with benzoate- or succinate-adapted cells revealed the specific abundance increase of substrate-specific protein sets. Their coding genes form distinct clusters on the genome, two of which were assigned to 4-methylbenzoate and one to benzoate degradation. The predicted functions of the gene products agree with a specific 4-methylbenzoyl-CoA degradation pathway in addition to and analogous to the known anaerobic benzoyl-CoA degradation pathway. In vitro benzoyl-CoA and 4-methylbenzoyl-CoA reductase activities revealed the electron donor and ATP-dependent formation of the corresponding conjugated cyclic dienoyl-CoA/4-methyl-dienoyl-CoA products. The 4-methylbenzoyl-CoA reductase activity was induced in the presence of 4-methylbenzoate. In accordance, metabolite analysis of cultures grown with 4-methylbenzoate tentatively identified 4-methylcyclohex-1,5-diene-1-carboxylate. The 4-methylbenzoate induced genes were assigned to code for the putative 4-methylbenzoyl-CoA reductase; their products display pronounced sequence disparity from the conventional class I benzoyl-CoA reductase, which does not accept substituents at the para-position. Identification of 3-methylglutarate together with the formation of specific proteins for ring cleavage and β-oxidation in 4-methylbenzoate-adapted cells suggest conservation of the methyl group along the specific 4-methylbenzoyl-CoA degradation pathway.