NSUN2 (E9Y5E) Rabbit mAb #52901

Chemical modifications of RNA regulate many cellular processes. One particular RNA modification, 5-methylcytosine (5-mC), regulates ribosome assembly, translation, and RNA stability (1). In eukaryotes, this modification is added to RNA by the DNA methyltransferase homologue 2 protein (DNMT2; also known as TRDMT1), and also by members of the NOL1/NOP2/SUN domain (NSUN) family of proteins. NSUN proteins are putative S-adenosylmethionine (SAM)-dependent methyltransferases that carry out their enzymatic activity by utilizing two cysteine residues in their active sites (2). There are currently seven known members of this family, consisting of NOP2 (NSUN1) and NSUN2-7.

NSUN2 is an 86 kDa member of the NSUN family that is predominantly localized to the nucleus and methylates a variety of tRNAs and other RNA substrates (3). NSUN2 has been found to play a role in the methylation of pre-tRNA^Leu, tRNA^Gly, tRNA^Val, tRNA^Leu, and tRNA^Asp (1,4,5). It has also been found to methylate mRNAs and several ncRNAs, such as vtRNAs (6-8). Elevated NSUN2 protein levels have been reported in multiple types of human cancers, including breast, prostate, kidney, bladder, and liver, among others (9). The methyltransferase activity of NSUN2 is reduced upon Aurora B kinase-mediated phosphorylation at Ser139 (10), and there is potential for NSUN2 to be used as a therapeutic target or diagnostic marker for Aurora B linked cancers (9).