Modification of Protein in the system

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Protein arginine methyltransferases are a family of enzymes that can behave as catalysts in arginine methylation. Arginine methylation is the modification of the posttranslational protein that can be found in the eukaryotic cells. There are different types of protein arginine methyltransferases, and the main aim of this study is the protein arginine methyltransferase-four. They are spread all over the bodies of mammals and humans, including neurons. Protein arginine methyltransferase-four was made from the process that saw it bound to a steroid receptor co-activator, glutamate receptor interacting protein-one. It is also called the co-activator and associated arginine methyltransferase-one. Protein arginine methyltransferase-four serves in several cellular processes such as transcription, cell cycle progression, and in the deoxyribonucleic acid damage response. It is an I type arginine methyltransferase with unknown substrate methylation motif which makes it different from other I type protein arginine methyltransferases (Singh, Mori, Miyata, Tohyama, & Ramamurthy, 2013).

Enzyme Cellular Functioning and in Disease State

Co-activator-associated arginine methyltransferase-one performs a task in ensuring the cell proliferation and survival is regulated, within the tumor cells. This happened when protein arginine methyltransferase-four interacts and cooperates with the proteins that are related to cancer. In this process, co-activator-associated arginine methyltransferase-one acts as a transcriptional co-activator that helps regulate the expression of the cyclin protein. Protein arginine methyltransferase-four is essential in the proliferation of breast cancer cells. Baldwin, Morettin, & Côté, (2014) explain that this happens through the methylation process that is stimulated by estrogen hormones. This enzyme further acts as the regulator of activity and stability of amplified in breast-one. Amplified in breast-one is a transcriptional co-activator which usually is overexpressed in the breast tumors. In as much as protein arginine methyltransferase-four helps in cancer issues, it is critical to note that its overexpression in breast cancer cells limits the growth of cells that are stimulated by estrogen.
Amongst the many transcriptional factors, nuclear factor stands out as an important feature because of its use in the regulation of transcription of proteins that are involved in the inflammatory diseases, immunity development, and septic shock. The transcription factor of the nuclear factor constitutes of homodimers or heterodimers of subunits. The proteins have a relatively high amount of Rel homology domain that is conserved, which is composed of a lot of amino acids. This conserved domain performs major tasks in the form of heterologous or homologous dimerization, translocating the nuclear, and acts as a deoxyribonucleic acid binder. Co-activator-associated arginine methyltransferase-one acts as a co-activator through controlling transcription in a manner that is gene-specific and by improving the process of recruitment of the nuclear factor that helps in cognation of sites (Kim, Yoo, Yang, Kim, Hong, & Cho, 2016).
Protein arginine methyltransferase-four is highly expressed in the hematopoietic progenitor cells. In these cells, the co-activator-associated arginine methyltransferase-one acts as an inhibitor of the differentiation of myeloid. This happens through the process of methylation of runt-related transcription factor one where the zinc finger protein-two genes are eventually assembled. The protein arginine methyltransferase-four reduces, regarding their expression, with time as the hematopoietic progenitor cells undergo myeloid differentiation. The resultant effect herein is that the zinc finger protein-two genes are reduced at the promoter points of the micro ribonucleic acids. Vu, Perna, Wang, Voza, Figueroa, Tempst, & Deblasio, (2013) explain that the micro ribonucleic acids after that are afforded a chance of transcription. A further upward regulation of micro ribonucleic acids allows for more of these acids to be expressed. This upward regulation is possible because of the ability of the micro ribonucleic acids to target the three prime, untranslated regions of the protein arginine methyltransferase-four. The upward regulation of the micro ribonucleic acids results in the reduction in the co-activator-associated arginine methyltransferase-one and these results into the sustainability of the process of myeloid differentiation.
Protein arginine methyltransferase-four plays a primary role of muscle differentiation in animals. The process of differentiating skeletal muscles entails the muscle regulatory factors cooperating with Myod, Myogenin, Myogenic factor-five, Myogenic regulatory factor-four, members of the Myocyte-enhancer factor-two family, and chromatin remodeling enzymes. A lot of enzymes including the protein arginine methyltransferases family are usually used to modify histone. These enzymes regulate the myogenic genes in cell culture. Protein arginine methyltransferase-four and protein arginine transferase-five are particularly the two enzymes that take part in the skeletal muscle differentiation because they are essential for the myogenic processes. This happens when co-activator-associated arginine methyltransferase-ones methylate histone residues on the residues of arginine that are specific so that the transcription can be regulated. Non-histone proteins like the transcriptional coactivators as well, are methylated. In as much as it has been a stumbling block clearly explaining the mechanisms that the protein arginine methyltransferase-four uses in the myogenic processes, it is evident that it plays a crucial role in ensuring there is muscle differentiation. To prove this, Batut, Duboe, & Vandel, (2011) discuss an experimental example where the translation of the co-activator-associated arginine methyltransferase-one enzymes is interfered with using antisense morpholinos. The introduction of the morpholinos in the translation reduces the enzymes to a large extent. The co-activator-associated arginine methyltransferase-one morphants exhibit small round somites after the interruption of the translation process. The round shape suggests that the protein co-activator-associated arginine methyltransferase-one can be involved in the muscle progenitor cells elongations, which are usually round in shape initially. For protein arginine methyltransferase-five the situation would be different in that a flat and long somite would be exhibited. This is a clear indication of the specificity of these enzymes in the myogenic processes. This shows how much important the protein arginine methyltransferase-four together with the protein arginine methyltransferase-five enzymes are to the myogenic processes.

Conclusion

It is critical to understand that the protein arginine methyltransferase-four plays a significant role in the body cells of eukaryotes. A lot of the enzymes in the body have different unique functions, and that is why they will often look different in some ways. Co-activator-associated arginine methyltransferase-one has a crucial task in ensuring the sustainability of the myeloid process. Breast cancer and cancer, in general, have a connection with protein arginine methyltransferase4 in the sense that this enzyme helps reduce or eliminate cancer. However, an overexpression of this enzyme can be hazardous because it promotes the limitation of growth of cells that are estrogen-related. Co-activator-associated arginine methyltransferase-one is critical in the muscle differentiation process. The histone and non-histone residues and proteins are the main ingredients for this process to be a success because they are methylated by the protein arginine methyltransferase-four enzyme. It is an important enzyme in the bodies of animals and thus its cellular functions give rise to crucial processes of the animals.

References

Baldwin, R. M., Morettin, A., & Côté, J. (2014). Role of PRMTs in cancer: Could minor isoforms be leaving a mark. World J Biol Chem, 5(2), 115-29.
Batut, J., Duboe, C., & Vandel, L. (2011). The methyltransferases PRMT4/CARM1 and PRMT5 control differentially myogenesis in zebrafish. PLoS One, 6(10), e25427.
Kim, J. H., Yoo, B. C., Yang, W. S., Kim, E., Hong, S., & Cho, J. Y. (2016). The Role of Protein Arginine Methyltransferases in Inflammatory Responses. Mediators of inflammation, 2016.
Singh, R., Mori, Y., Miyata, S., Tohyama, M., & Ramamurthy, V. (2013). Retinal Horizontal cell numbers are modulated by neuron specific methyl transferase, PRMT8. Investigative Ophthalmology & Visual Science, 54(15), 2450-2450.
Vu, L. P., Perna, F., Wang, L., Voza, F., Figueroa, M. E., Tempst, P. ... & Deblasio, T. (2013). PRMT4 blocks myeloid differentiation by assembling a methyl-RUNX1-dependent repressor complex. Cell reports, 5(6), 1625-1638.

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