Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase

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...

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Autores principales:	Darja Deobald, Lorenz Adrian, Christian Schöne, Michael Rother, Gunhild Layer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c37f66b8b000441589257bda3f49c408
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spelling	oai:doaj.org-article:c37f66b8b000441589257bda3f49c4082021-12-02T16:07:51ZIdentification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase10.1038/s41598-018-25716-x2045-2322https://doaj.org/article/c37f66b8b000441589257bda3f49c4082018-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-25716-xhttps://doaj.org/toc/2045-2322Abstract 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.Darja DeobaldLorenz AdrianChristian SchöneMichael RotherGunhild LayerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Darja Deobald Lorenz Adrian Christian Schöne Michael Rother Gunhild Layer Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
description	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.
format	article
author	Darja Deobald Lorenz Adrian Christian Schöne Michael Rother Gunhild Layer
author_facet	Darja Deobald Lorenz Adrian Christian Schöne Michael Rother Gunhild Layer
author_sort	Darja Deobald
title	Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
title_short	Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
title_full	Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
title_fullStr	Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
title_full_unstemmed	Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase
title_sort	identification of a unique radical sam methyltransferase required for the sp3-c-methylation of an arginine residue of methyl-coenzyme m reductase
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/c37f66b8b000441589257bda3f49c408
work_keys_str_mv	AT darjadeobald identificationofauniqueradicalsammethyltransferaserequiredforthesp3cmethylationofanarginineresidueofmethylcoenzymemreductase AT lorenzadrian identificationofauniqueradicalsammethyltransferaserequiredforthesp3cmethylationofanarginineresidueofmethylcoenzymemreductase AT christianschone identificationofauniqueradicalsammethyltransferaserequiredforthesp3cmethylationofanarginineresidueofmethylcoenzymemreductase AT michaelrother identificationofauniqueradicalsammethyltransferaserequiredforthesp3cmethylationofanarginineresidueofmethylcoenzymemreductase AT gunhildlayer identificationofauniqueradicalsammethyltransferaserequiredforthesp3cmethylationofanarginineresidueofmethylcoenzymemreductase
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Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase

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