Journal
FEBS LETTERS
Volume 591, Issue 12, Pages 1641-1652Publisher
WILEY
DOI: 10.1002/1873-3468.12649
Keywords
citrate synthase; metabolons; METTL12; mitochondria; protein methylation; substrate channelling
Funding
- Medical Research Council of the United Kingdom [MC_U1065663150, MR/M009858/1]
- Swiss Novartis Foundation
- MRC [MC_UU_00015/8, MC_EX_MR/M009858/1, MC_U105663150] Funding Source: UKRI
- Medical Research Council [MC_EX_MR/M009858/1, MC_U105663150, MC_UU_00015/8] Funding Source: researchfish
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The protein methylome in mammalian mitochondria has been little studied until recently. Here, we describe that lysine-368 of human citrate synthase is methylated and that the modifying enzyme, localized in the mitochondrial matrix, is methyltransferase-like protein 12 (METTL12), a member of the family of 7-strand methyltransferases. Lysine-368 is near the active site of citrate synthase, but removal of methylation has no effect on its activity. In mitochondria, it is possible that some or all of the enzymes of the citric acid cycle, including citrate synthase, are organized in metabolons to facilitate the channelling of substrates between participating enzymes. Thus, possible roles for the methylation of Lys-368 are in controlling substrate channelling itself, or in influencing protein-protein interactions in the metabolon.
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