Abstract
Human METTL20 methylates lysine residues adjacent to the recognition loop of the electron transfer flavoprotein in mitochondria
Highlights
The electron transfer flavoprotein (ETF) is a mobile electron carrier coupling mitochondrial fatty acid oxidation to respiration
We have found that another mitochondrial protein, the -subunit of the electron transfer flavoprotein (ETF) is methylated
It acts as a mobile electron carrier in the matrix of mitochondria, linking 11 different mitochondrial FAD-containing acyl-CoA dehydrogenases involved in fatty acid -oxidation to the ubiquinone pool of the respiratory chain [30, 31]
Summary
The electron transfer flavoprotein (ETF) is a mobile electron carrier coupling mitochondrial fatty acid oxidation to respiration. The ETF is a heterodimeric complex of ␣- and -subunits, known as ETF␣ and ETF, respectively (26 –29) It acts as a mobile electron carrier in the matrix of mitochondria, linking 11 different mitochondrial FAD-containing acyl-CoA dehydrogenases involved in fatty acid -oxidation to the ubiquinone pool of the respiratory chain [30, 31]. The location of the methylated lysine residues characterized in the current study, immediately adjacent to the recognition loop, suggests that their methylation may influence the interactions of the ETF with the dehydrogenases and possibly with ETF-quinone oxidoreductase, and that it could provide a mechanism of regulating the -oxidation of fatty acids. No protein lysine methyltransferase had been characterized previously in mitochondria
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