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 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
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Scientific reports. - 8 (2018) , 7404, ISSN: 2045-2322
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Freiburg
- (who)
-
Universität
- (when)
-
2023
- Creator
- Contributor
-
Lehrstuhl der Pharmazeutischen Biologie & Biotechnologie, AG Prof. Dr. G. Layer
- DOI
-
10.1038/s41598-018-25716-x
- URN
-
urn:nbn:de:bsz:25-freidok-2357388
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:43 PM CET
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Deobald, Darja
- Adrian, Lorenz
- Schöne, Christian
- Rother, Michael
- Layer, Gunhild
- Lehrstuhl der Pharmazeutischen Biologie & Biotechnologie, AG Prof. Dr. G. Layer
- Universität
Time of origin
- 2023
Other Objects (12)
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
The residue of uniqueness
Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase
Structure and function of the unusual tungsten enzymes acetylene hydratase and class II benzoyl-coenzyme A reductase
A cobalamin‐dependent radical SAM enzyme catalyzes the unique Cα‐methylation of glutamine in methyl‐coenzyme M reductase
On the evolution of coenzyme biosynthesis
Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis
Mechanisms of the 3-hydroxyl-3-methylglutaryl-coenzyme A reductase inhibitor-induced myotoxicity in human skeletal muscle cell cultures
Nitrate Reductase Precursor: Synthesis of Nitrate Reductase in Chlorella
The class II benzoyl-coenzyme A reductase complex from the sulfate-reducing Desulfosarcina cetonica
Nitrate Reductase of Chlorella Pyrenoidosa
[Properties of a] Nitrate Reductase of Chlorella
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
The residue of uniqueness
Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase
Structure and function of the unusual tungsten enzymes acetylene hydratase and class II benzoyl-coenzyme A reductase
A cobalamin‐dependent radical SAM enzyme catalyzes the unique Cα‐methylation of glutamine in methyl‐coenzyme M reductase
On the evolution of coenzyme biosynthesis
Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis
Mechanisms of the 3-hydroxyl-3-methylglutaryl-coenzyme A reductase inhibitor-induced myotoxicity in human skeletal muscle cell cultures
Nitrate Reductase Precursor: Synthesis of Nitrate Reductase in Chlorella
The class II benzoyl-coenzyme A reductase complex from the sulfate-reducing Desulfosarcina cetonica
Nitrate Reductase of Chlorella Pyrenoidosa
[Properties of a] Nitrate Reductase of Chlorella
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
The residue of uniqueness
Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase
Structure and function of the unusual tungsten enzymes acetylene hydratase and class II benzoyl-coenzyme A reductase
A cobalamin‐dependent radical SAM enzyme catalyzes the unique Cα‐methylation of glutamine in methyl‐coenzyme M reductase
On the evolution of coenzyme biosynthesis
Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis
Mechanisms of the 3-hydroxyl-3-methylglutaryl-coenzyme A reductase inhibitor-induced myotoxicity in human skeletal muscle cell cultures
Nitrate Reductase Precursor: Synthesis of Nitrate Reductase in Chlorella
The class II benzoyl-coenzyme A reductase complex from the sulfate-reducing Desulfosarcina cetonica
Nitrate Reductase of Chlorella Pyrenoidosa