Uncovering human METTL12 as a mitochondrial methyltransferase that modulates citrate synthase activity through metabolite-sensitive lysine methylation

  title={Uncovering human METTL12 as a mitochondrial methyltransferase that modulates citrate synthase activity through metabolite-sensitive lysine methylation},
  author={Jędrzej M. Małecki and Magnus E. Jakobsson and Angela Yeuan Yen Ho and Anders Moen and Arild C. Rustan and P{\aa}l {\O}. Falnes},
  journal={The Journal of Biological Chemistry},
  pages={17950 - 17962}
Lysine methylation is an important and much-studied posttranslational modification of nuclear and cytosolic proteins but is present also in mitochondria. However, the responsible mitochondrial lysine-specific methyltransferases (KMTs) remain largely elusive. Here, we investigated METTL12, a mitochondrial human S-adenosylmethionine (AdoMet)-dependent methyltransferase and found it to methylate a single protein in mitochondrial extracts, identified as citrate synthase (CS). Using several in vitro… 

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    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2019
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