Human TRMT112-Methyltransferase Network Consists of Seven Partners Interacting with a Common Co-Factor.
Baiba BrūmeleMargit MutsoLilian TelanneKadri ÕunapKarīna SpundeAare AbroiReet KurgPublished in: International journal of molecular sciences (2021)
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.
Keyphrases
- amino acid
- genome wide
- induced apoptosis
- dna methylation
- cell cycle arrest
- binding protein
- protein protein
- endothelial cells
- transcription factor
- gene expression
- oxidative stress
- hiv testing
- cell death
- cell proliferation
- hydrogen peroxide
- hepatitis c virus
- network analysis
- protein kinase
- toll like receptor
- induced pluripotent stem cells