Protein arginine methyltransferases

Protein phosphatase 2C Protein arginine methyltransferase Protein arginine methyltransferase Arylalkylamine N-acetyltransferase SARS Cov 3C-like protease AHAS... 

Amur SG, Shanker G, Cochran JM, Ved HS, Pieringer RA (1986) Correlation between inhibition of myelin basic protein (arginine) methyltransferase by sinefungin and lack of compact myelin formation in cultures of cerebral cells from embryonic mice. J Neurosci Res 16 367-376 An W, Kim J, Roeder RG (2004) Ordered cooperative functions of PRMTl, p300, and CARMl in transcriptional activation by p53. Celll 17 735-748... 

Cheng D, Yadav N, King RW, Swanson MS, Weinstein EJ, Bedford MT (2004) Small molecule regulators of protein arginine methyltransferases. J Biol Chem 279 23892—23899... 

Lee, J.H., Cook, J.R. and Pesfka, S. (2007) Protein arginine methyltransferases Evolution and assessment of then-pharmacological and therapeutic potential. Pharmacology ej Therapeutics, 113 (1), 50-87. 

Zhang, X. and Cheng, X. (2003) Structure of the Predominant Protein Arginine Methyltransferase PRMTl and Analysis of Its Binding to Substrate Peptides. Structure (Camb), 11 (5), 509-520. 

Zhang, X., Zhou, L. and Cheng, X. (2000) Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. The EM BO Journal, 19 (14), 3509-3519. 

Histone methylation by methyltransferases is another vddely described modification that also plays an important role in regulation of transcriptional activity. Methylation can occur either on arginine or on lysine residues in the N-termini of histones and therefore this group of enzymes can be separated into protein arginine methyltransferases (PRMTs) and lysine methyltransferases (KMTs). 

Pahlich, S., Bschir, K, Chiavi, C., Belyanskaya, L. and Gehring, H. (2005) Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide. Proteins, 61, 164—175. 

Miranda, T.B., Miranda, M., Frankel, A. and Clarke, S. (2004) PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. The Journal of Biological Chemistry, 279, 22902-22907. 

Meyer, R., Wolf, S.S. and Obendorf M. (2007) PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor. The Journal of Steroid Biochemistry and Molecular Biology, 107, 1-14. 

Dacwag, C.S., Ohkawa, Y, Pal, S., Sif S. and Imbalzano, A.N. (2007) The protein arginine methyltransferase Prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling. Molecular and Cellular Biology, 27, 384-394. 

Osborne, T., Roska, R.L., Rajski, S.R. and Thompson, P.R. (2008) In Situ Generation of a Bisubstrate Analogue for Protein Arginine Methyltransferase 1. Journal of the American Chemical Society (in press). 

Wang R, Zheng W, Yu H et al (2011) Labeling substrates of protein arginine methyltransferase with engineered enzymes and matched S-adenosyl-L-methionine analogues. J Am Chem Soc 133 7648-7651... 

Pal S, Sif S. Interplay between chromatin remodelers and protein arginine methyltransferase s. J. CeU Physiol. 2007 213 306-315. 48. 

Protein (arginine) Methyltransferase. The enzyme(s) which methylates arginine residues of proteins was named protein methylase I by Paik and Kim (202). The recommended name is protein (arginine) methyltransferase (S-adenosyl-L-methionine protein N-methylttransferase, EC 2.1.1.23). The enzyme(s) catalyzes the reaction... 

Just as with protein (arginine) methyltransferase, it is likely that there are several protein (lysine) methyltransferases. Neurospora and wheat germ cytochrome cs contain only c-N-trimethyllysine (196), while pea embryo histone III and bovine retina opsin contain either c-N-mono-or c-N-dimethyllysine, but not c-N-trimethyllysine (211). Flagella protein from Salmonella serpens contains only c-N-monomethyllysine (212). 

Similarly, histone arginine/lysine methylation can be the target for the development of therapeutics. The status of histone arginine methylation is intimately involved in gene transcription. Recently, several compounds were found to inhibit protein arginine methyltransferases (PRMTs) [54]. It can also be interesting to explore how this small molecule could be exploited for developing therapeutics. 

The identities of several protein arginine methyltransferases are now known, but only a few have been shown to have specificity for histone proteins. The mammalian PRMT1, JBP1, and CARMI, as well as the Saccharomyces Rmtl, have histone methyltransferase activity (McBride and Silver, 2001). However, the catalytic mechanism for the methyl group transfer as well as the makeup of the active sites of PRMTs differ somewhat from SET domain proteins. 

Fig. 7. Sequence alignment of known protein arginine methyltransferases (PRMTs). Sequences essential for AdoMet and substrate binding are indicated by blue and red bars. (See Color Insert.)...

Gary, J. D. et al. (1996). The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J. Biol. Chem. 271(21), 12585-12594. 

Teyssier, C., Chen, D., and Stallcup, M. R. (2002). Requirement for multiple domains of the protein arginine methyltransferase CARMI in its transcriptional coactivator function./. Biol. Chem. 277(48), 46066-46072. 

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