Publication Details

Reference Category Journals
DOI / URL link
Title (Primary) Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
Author Deobald, D.; Adrian, L.; Schöne, C.; Rother, M.; Layer, G.;
Journal Scientific Reports
Year 2018
Department ISOBIO;
Volume 8
Language englisch;
POF III (all) T41;
Supplements https://static-content.springer.com/esm/art%3A10.1038%2Fs41598-018-25716-x/MediaObjects/41598_2018_25716_MOESM1_ESM.pdf
Abstract The biological formation of methane (methanogenesis) is a globally important process, which is exploited in biogas technology, but also contributes to global warming through the release of a potent greenhouse gas into the atmosphere. The last and methane-releasing step of methanogenesis is catalysed by the enzyme methyl-coenzyme M reductase (MCR), which carries several exceptional posttranslational amino acid modifications. Among these, a 5-C-(S)-methylarginine is located close to the active site of the enzyme. Here, we show that a unique Radical S-adenosyl-L-methionine (SAM) methyltransferase is required for the methylation of the arginine residue. The gene encoding the methyltransferase is currently annotated as “methanogenesis marker 10” whose function was unknown until now. The deletion of the methyltransferase gene ma4551 in Methanosarcina acetivorans WWM1 leads to the production of an active MCR lacking the C-5-methylation of the respective arginine residue. The growth behaviour of the corresponding M. acetivorans mutant strain and the biophysical characterization of the isolated MCR indicate that the methylated arginine is important for MCR stability under stress conditions.
ID 20618
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=20618
Deobald, D., Adrian, L., Schöne, C., Rother, M., Layer, G. (2018):
Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
Sci. Rep. 8 , art. 7404