PRMTs

Background PRMT7 is a type III protein arginine methyltransferase that monomethylates arginine residues mainly within the RXR motif (Fig.1) (PIMID: 24247247). PRMT7 was shown to play an important role in muscle physiology, stem cell biology, and cellular stress response (PIMID: 32409666, 27225728, 26854227).  Fig.1. Mammalian PRMTs. There are 9 members and 3 types of the Read More …

Background PRMT8 is type I protein arginine methyltransferase expressed mainly in the brain, which mono- and asymmetrically dimethylates histone and nonhistone proteins (Fig.1). It shares over 80% of amino acid sequence homology with PRMT1. At the N-terminus, it harbors a glycine that can be myristoylated which results in its plasma membrane localization (PIMID: 16051612). Fig.1. Read More …

Background PRMT3 is type I protein arginine methyltransferase which mono- and asymmetrically dimethylates proteins, mainly in glycine and arginine-rich motifs (Fig.1, PIMID: 15175657). Fig.1. Mammalian PRMTs. There are 9 members and 3 types of the PRMT family. Type I, II and III PRMTs catalyze the formation of monomethyl arginines (Rme1). Type I PRMTs catalyze asymmetric arginine Read More …

Background PRMT6 is type I protein arginine methyltransferase which mono- and asymmetrically dimethylates histone and nonhistone proteins, mainly in glycine and arginine rich motifs (Fig.1). PRMT6 shows predominant nuclear localization and is implicated in the regulation of nuclear processes such as DNA repair and gene expression (PIMID: 11724789, 18079182).  Fig.1. Mammalian PRMTs. There are 9 Read More …

Background PRMT5 in complex with the WD-repeat protein MEP50 is the major type II protein arginine methyltransferase responsible for mono- and symmetric dimethylation of arginine in a great variety of proteins (Fig.1). It plays a critical role in diverse cellular processes such as genome organization, transcription, translation, differentiation, cell cycle, DNA repair,  RNA processing, and Read More …

Background PRMT1 is the type I protein arginine methyltransferase (Fig.1) which mono- and asymmetrically dimethylates histone and nonhistone proteins, mainly in glycine and arginine-rich motifs and is involved in various cellular processes such as transcription, RNA processing, DNA repair, cell cycle or signal transduction (PMID:26612103). It is responsible for depositing over 90% of the total Read More …

We have used the PTMScan® Mono-Methyl Arginine Motif [mme-RG] Kit #12235 from CST in order to determine novel PRMT7 substrates. In preliminary experiments done few years ago by our pharma partner several novel potential PRMT7 substrates were discovered with the kit, including HSP70, which was further validated by different methods (https://www.biorxiv.org/content/10.1101/503136v2). In order to obtain biological replicates, Read More …