Journal
SCIENTIFIC REPORTS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-018-19615-4
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Funding
- Program for Development of New Functional Antibody Technologies of the New Energy and Industrial Technology Development Organization (NEDO) of Japan
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Naito Foundation
- Inamori Grant Program
- Takeda Science Foundation
- Uehara Memorial Foundation
- RIKEN internal research fund
- Grants-in-Aid for Scientific Research [17K07144, 17K18719] Funding Source: KAKEN
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METTL20 is a seven-beta-strand methyltransferase that is localised to the mitochondria and tri-methylates the electron transfer flavoprotein (ETF) beta subunit (ETFB) at lysines 200 and 203. It has been shown that METTL20 decreases the ability of ETF to extract electrons from medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) and glutaryl-CoA dehydrogenase in vitro. METTL20-mediated methylation of ETFB influences the oxygen consumption rate in permeabilised mitochondria, suggesting that METTL20-mediated ETFB methylation may also play a regulatory role in mitochondrial metabolism. In this study, we generated Mettl20 knockout (KO) mice to uncover the in vivo functions of METTL20. The KO mice were viable, and a loss of ETFB methylation was confirmed. In vitro enzymatic assays revealed that mitochondrial ETF activity was higher in the KO mice than in wild-type mice, suggesting that the KO mice had higher beta-oxidation capacity. Calorimetric analysis showed that the KO mice fed a ketogenic diet had higher oxygen consumption and heat production. A subsequent cold tolerance test conducted after 24 h of fasting indicated that the KO mice had a better ability to maintain their body temperature in cold environments. Thus, METTL20 regulates ETF activity and heat production through lysine methylation when beta-oxidation is highly activated.
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