作者: Jędrzej Małecki , Angela Y. Y. Ho , Anders Moen , Helge-André Dahl , Pål Ø. Falnes
关键词: Protein targeting 、 Biochemistry 、 Histone methyltransferase 、 Histone 、 Protein methylation 、 Methylation 、 Methyltransferase 、 Electron-transferring flavoprotein 、 Lysine 、 Biology
摘要: Proteins are frequently modified by post-translational methylation of lysine residues, catalyzed S-adenosylmethionine-dependent methyltransferases (KMTs). Lysine histone proteins has been extensively studied, but it recently become evident that non-histone is also abundant and important. The human methyltransferase METTL20 belongs to a group 10 established putative KMTs. We here found be associated with mitochondria determined recombinant methylated single protein in extracts from cells. Using an activity-based purification scheme, we identified the β-subunit mitochondrially localized electron transfer flavoprotein (ETFβ) as substrate METTL20. Furthermore, was specifically methylate two adjacent Lys(200) Lys(203), ETFβ both vitro Interestingly, residues partially overlap so-called "recognition loop" ETFβ, which shown mediate its interaction various dehydrogenases. Accordingly, METTL20-mediated reduced ability receive electrons medium chain acyl-CoA dehydrogenase glutaryl-CoA dehydrogenase. In conclusion, present study establishes first KMT suggests may regulate cellular metabolism through modulating between Based on previous naming similar enzymes, suggest renaming ETFβ-KMT.