Toward Understanding Molecular Recognition between PRMTs and their Substrates
Owen M. Price, Joan M. Hevel
Abstract
Protein arginine methylation is a widespread eukaryotic posttranslational modification that occurs with as much frequency as ubiquitinylation. Yet, how the nine different human protein arginine methyltransferases (PRMTs) recognize their respective protein targets is not well understood. This review summarizes the progress that has been made over the last decade or more to resolve this significant biochemical question. A multipronged approach involving structural biology, substrate profiling, bioorthogonal chemistry and proteomics is discussed.
Topics & Concepts
MethyltransferaseMethylationProfiling (computer programming)Protein arginine methyltransferase 5Posttranslational modificationProteomicsArginineBioorthogonal chemistryComputational biologyBiochemistryBiologyChemistryEnzymeAmino acidComputer scienceCombinatorial chemistryClick chemistryGeneOperating systemCancer-related gene regulationEpigenetics and DNA Methylation