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- W4200470594 abstract "Methylation is an essential epigenetic modification mainly catalysed by S-Adenosyl methionine-dependent methyltransferases (MTases). Several MTases require a cofactor for their metabolic stability and enzymatic activity. TRMT112 is a small evolutionary conserved protein that acts as a co-factor and activator for different MTases involved in rRNA, tRNA and protein methylation. Using a SILAC screen, we pulled down seven methyltransferases-N6AMT1, WBSCR22, METTL5, ALKBH8, THUMPD2, THUMPD3 and TRMT11-as interaction partners of TRMT112. We showed that TRMT112 stabilises all seven MTases in cells. TRMT112 and MTases exhibit a strong mutual feedback loop when expressed together in cells. TRMT112 interacts with its partners in a similar way; however, single amino acid mutations on the surface of TRMT112 reveal several differences as well. In summary, mammalian TRMT112 can be considered as a central hub protein that regulates the activity of at least seven methyltransferases." @default.
- W4200470594 created "2021-12-31" @default.
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- W4200470594 date "2021-12-18" @default.
- W4200470594 modified "2023-10-17" @default.
- W4200470594 title "Human TRMT112-Methyltransferase Network Consists of Seven Partners Interacting with a Common Co-Factor" @default.
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- W4200470594 doi "https://doi.org/10.3390/ijms222413593" @default.
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