Protein Methylase II

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Protein methylesterase II, also known as heterogeneous ribonucleoprotein-M methyltransferase, was first discovered by Lee and colleagues in 1996. The enzyme was identified in HeLa cells and was found to be localized in the nucleus where it regulates various gene expression pathways. Protein methylesterase II (PRMT2), a member of the protein arginine methylation transferase (PRMT) family, is responsible for the transfer of a methyl group from S-adenosyl-l-methionine (SAM) to the guanidine group of arginine residues in proteins. In this article, we will explore the background, structure, function, mechanism, clinical implications and applications of protein methylesterase II.

Structure

PRMT2 is a monomeric protein consisting of 356 amino acid residues with a molecular weight of approximately 40 kDa. The enzyme contains two distinct structural domains: an N-terminal alpha helix structural domain and a central catalytic structural domain. The catalytic structural domain contains three conserved regions, called h1, h2 and h3, which are involved in the binding of SAM and arginine substrates.

Functions

PRMT2 is involved in various biological processes, including gene expression, RNA processing, protein translocation and cytoskeleton dynamics. It is known to regulate gene expression by regulating RNA splicing and protein translation. This enzyme regulates the production of alternative splice isoforms, which have a significant impact on protein function.

Mechanism

PRMT2 transfers a methyl group from SAM to the guanidine group of an arginine residue in a protein, producing a monomethylated arginine (MMA) or a symmetrical dimethylarginine (SDMA) residue. Methylation of arginine residues has been shown to play a key role in protein-protein interactions, RNA processing, DNA repair, and signal transduction. PRMT2 belongs to the type II PRMT subgroup, which preferentially generates SDMA residues. The catalytic mechanism of PRMT2 involves the formation of a complex between itself, SAM, and the substrate protein. The enzyme interacts with the substrate protein through a conserved arginine-binding groove where it methylates the arginine residue. The preference for SDMA over MMA is determined by the substrate residues flanking the target arginine residue.

Clinical Significance

PRMT2 is clinically important and has been associated with many diseases, including cancer, neurological disorders and infectious diseases. Studies have shown that PRMT2 expression is altered in a variety of cancers, including breast, lung, prostate and liver cancers. The enzyme regulates the expression of various oncogenes and tumor suppressor genes, making it a potential target for cancer therapy. PRMT2 has also been identified as a potential target for the development of therapies for neurological disorders such as Huntington's disease and Alzheimer's disease.

Applications

PRMT2 has a number of practical applications in the fields of drug discovery and protein engineering. The enzyme could be utilized in drug discovery for the ability to screen compounds to selectively target PRMT2. This could lead to the development of drugs that can selectively target the enzyme, potentially leading to the development of more effective cancer treatments.

Conclusion

PRMT2 is an important enzyme involved in various biological processes that regulate gene expression and protein function. Its importance in a variety of diseases has been demonstrated, making it a potential target for drug discovery and therapeutic intervention. The structure, function and mechanism of action of this enzyme have been extensively studied, enabling researchers to develop targeted therapeutic approaches and to utilize the enzyme for practical applications in drug discovery and protein engineering. Continued research and development of PRMT2 holds great promise in the development of medicine and biotechnology.