PhD Student Khalifa University, United Arab Emirates
Abstract: Methyltransferases are group of enzymes that catalyze the addition of methyl alkyl group to their clients. They play a critical role in cell homeostasis as they are involved in epigenetic, epitranscriptomic, and post-translational modifications. Such events control gene expression, RNA splicing, and protein-protein interactions. Recently, it was found that glucose affects the machinery of methyltransferases. For example, glucose was found to modify epigenomics by inhibiting DNA methyltransferase 1 (DNMT1). It can also mediate oligomerization and catalytic events like what happens in NSUN2. Although glucose binding mode was not revealed yet in methyltransferases-glucose complexes, there is a trend that glucose forms hydrogen bonds with polar and charged amino acid residues, as well as phenyl and indole hydrophobic interactions with its ring. The electrostatic surface analysis of the glucose-binding residues in NSUN2 show that the majority of the region is polar, mainly due to Lysine, Arginine, and Glutamine. Sequence analysis with other human glucose sensitive proteins show conserved amino acids that might play a role in glucose sensing.
