PRMT5/MEP50 Complex (human, recombinant)

Protein-arginine N-methyltransferase 5 (PRMT5) is a type II PRMT and member of the class I S-adenosylmethionine-dependent methyltransferases that symmetrically dimethylates arginine residues in proteins and histones.¹ It is composed of an N-terminal TIM domain and a C-terminal catalytic domain. PRMT5 proteins interact with methylosome 50 (MEP50) proteins primarily via the TIM domain to form a hetero-octameric complex that is more active than PRMT5 alone.² Both PRMT5 and MEP50 are found in a wide variety of somatic and embryonic tissues, including the fetal ovary, fetal heart, and adult retina.³ The PRMT5-MEP50 complex methylates spliceosomal proteins and newly synthesized histone H2A in the cytoplasm and interacts with additional binding partners to regulate transcription through the methylation of NF-κB and p53 and other transcription factors in the nucleus. PRMT5 and MEP50 expression is increased in a variety of cancers and correlated with lower survival rates in patients with non-small cell lung cancer (NSCLC). Mutations in each gene are also associated with many types of cancer. Cayman's PRMT5-MEP50 protein can be used for enzyme activity assays.

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1. Antonysamy, S. The structure and function of the PRMT5:MEP50 complex. Macromolecular protein complexes 185-194 (2017).

2. Antonysamy, S., Bonday, Z., Campbell, R.M., et al. Crystal structure of the human PRMT5:MEP50 complex. Proc. Natl. Acad. Sci. USA 109(44), 17960-17965 (2012).

3. Stopa, N., Krebs, J.E., and Shechter, D. The PRMT5 arginine methyltransferase: Many roles in development, cancer and beyond. Cell Mol. Life Sci. 72(11), 2041-2059 (2015).