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  Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds

Kurth, J. M., Nobu, M. K., Tamaki, H., de Jonge, N., Berger, S., Jetten, M. S. M., et al. (2021). Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds. ISME JOURNAL. doi:10.1038/s41396-021-01025-6.

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Kurth, Julia M.1, Author
Nobu, Masaru K.1, Author
Tamaki, Hideyuki1, Author
de Jonge, Nadieh1, Author
Berger, Stefanie1, Author
Jetten, Mike S. M.1, Author
Yamamoto, Kyosuke1, Author
Mayumi, Daisuke1, Author
Sakata, Susumu1, Author
Bai, Liping1, Author
Cheng, Lei1, Author
Nielsen, Jeppe Lund1, Author
Kamagata, Yoichi1, Author
Wagner, T.2, Author           
Welte, Cornelia U.1, Author
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1external, ou_persistent22              
2Research Group Microbial Metabolism, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_3282402              

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 Abstract: Methane-generating archaea drive the final step in anaerobic organic compound mineralization and dictate the carbon flow of Earth's diverse anoxic ecosystems in the absence of inorganic electron acceptors. Although such Archaea were presumed to be restricted to life on simple compounds like hydrogen (H-2), acetate or methanol, an archaeon, Methermicoccus shengliensis, was recently found to convert methoxylated aromatic compounds to methane. Methoxylated aromatic compounds are important components of lignin and coal, and are present in most subsurface sediments. Despite the novelty of such a methoxydotrophic archaeon its metabolism has not yet been explored. In this study, transcriptomics and proteomics reveal that under methoxydotrophic growth M. shengliensis expresses an O-demethylation/methyltransferase system related to the one used by acetogenic bacteria. Enzymatic assays provide evidence for a two step-mechanisms in which the methyl-group from the methoxy compound is (1) transferred on cobalamin and (2) further transferred on the C-1-carrier tetrahydromethanopterin, a mechanism distinct from conventional methanogenic methyl-transfer systems which use coenzyme M as final acceptor. We further hypothesize that this likely leads to an atypical use of the methanogenesis pathway that derives cellular energy from methyl transfer (Mtr) rather than electron transfer (F420H2 re-oxidation) as found for methylotrophic methanogenesis.

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Language(s): eng - English
 Dates: 2021-06-18
 Publication Status: Published online
 Pages: 17
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Title: ISME JOURNAL
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 1751-7362