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• W4293764695 abstract "Abstract Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD + -dependent deacetylase sirtuin 3 (SIRT3), however it remains unclear whether corresponding mitochondrial acetyltransferases exist. We used a bioinformatics approach to search for mitochondrial proteins with an acetyltransferase catalytic domain, and identified a novel splice variant of ELP3 (mt-ELP3) of the elongator complex, which localizes to the mitochondrial matrix in mammalian cells. Unexpectedly, mt-ELP3 does not mediate mitochondrial protein acetylation but instead induces a post-transcriptional modification of mitochondrial-transfer RNAs (mt-tRNAs). Overexpression of mt-ELP3 leads to the protection of mt-tRNAs against the tRNA-specific RNase angiogenin, increases mitochondrial translation, and furthermore increases expression of OXPHOS complexes. This study thus identifies mt-ELP3 as a non-canonical mt-tRNA modifying enzyme." @default.
• W4293764695 created "2022-08-31" @default.
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• W4293764695 date "2022-08-31" @default.
• W4293764695 modified "2023-09-27" @default.
• W4293764695 title "A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function" @default.
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• W4293764695 doi "https://doi.org/10.1038/s41598-022-18114-x" @default.
• W4293764695 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36045139" @default.
• W4293764695 hasPublicationYear "2022" @default.
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