{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNRMT2, a close homolog of NRMT1, functions as an N-terminal methyltransferase that specifically targets the free α-amino group of proteins. While NRMT1 can catalyze mono-, di-, and trimethylation in a distributive manner, NRMT2 is primarily restricted to monomethylation. Both enzymes recognize the same N-terminal consensus sequences and display similar tissue expression and cellular localization, yet they differ in their catalytic roles. Notably, when NRMT1 and NRMT2 are co-expressed, NRMT2 enhances the formation of trimethylated substrates by priming them, thereby effectively activating NRMT1 and influencing DNA-protein interactions through this methylation process."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Janusz J Petkowski, Lindsay A Bonsignore, John G Tooley, et al. "}, {"type": "b", "children": [{"type": "t", "text": "NRMT2 is an N-terminal monomethylase that primes for its homologue NRMT1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20131163"}], "href": "https://doi.org/10.1042/BJ20131163"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24090352"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24090352"}]}]}]}