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Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism

Protein arginine N‐methyltransferases (PRMTs) are responsible for the transfer of one or two methyl groups from the methyl donor S‐adenosyl‐L‐methionine (SAM) to produce mono‐ or dimethylated arginine residues and the spent cofactor S‐adenosyl‐L‐homocysteine (SAH). Methylated arginines in eukaryotic cells are involved in several crucial biological processes, including transcription control, DNA damager repair, and RNA processing. However, contrasting findings for two major questions in the field have generated debate regarding PRMT mechanisms. The purpose of this research was to elucidate the PRMT1 mechanism and answer these two highly debated questions: do PRMTs dimethylate their substrates processively or distributively, and do PRMTs bind their substrates using a random or sequential method of substrate binding?