Recombinant Human PRMT1 Protein, N-His

Description of Recombinant Human PRMT1 Protein, N-His

Introduction

Recombinant human PRMT1 protein (protein arginine methyltransferase 1) is a key enzyme involved in the post-translational modification of proteins through the addition of methyl groups to arginine residues. This protein plays a crucial role in regulating various cellular processes, such as gene expression, cell signaling, and protein-protein interactions. In this article, we will discuss the structure, activity, and applications of recombinant human PRMT1 protein.

Structure of Recombinant Human PRMT1 Protein

Recombinant human PRMT1 protein is a 42 kDa protein that consists of 371 amino acids. It belongs to the PRMT family of enzymes, which are characterized by the presence of a highly conserved catalytic domain known as the “PRMT signature motif”. This motif is responsible for the catalytic activity of PRMT1 protein, and it is composed of three conserved regions, namely, the AdoMet binding site, the catalytic site, and the substrate binding site.

The crystal structure of recombinant human PRMT1 protein has been determined, revealing a compact fold with a central β-sheet surrounded by α-helices. The active site of the enzyme is located at the interface of the β-sheet and α-helices, where the AdoMet binding site and the catalytic site are in close proximity.

Activity of Recombinant Human PRMT1 Protein

Recombinant human PRMT1 protein is a type I PRMT enzyme, which catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to the guanidino nitrogen of arginine residues in target proteins. This process results in the formation of monomethylarginine (MMA) or asymmetric dimethylarginine (ADMA) residues on the target protein.

The activity of PRMT1 protein is regulated by various factors, such as its binding partners, post-translational modifications, and cellular localization. For instance, the interaction of PRMT1 with its binding partner, coactivator-associated arginine methyltransferase 1 (CARM1), enhances its methyltransferase activity. On the other hand, phosphorylation of PRMT1 by protein kinase A (PKA) inhibits its activity.

Applications of Recombinant Human PRMT1 Protein

Recombinant human PRMT1 protein has various applications in both basic research and drug discovery. Its ability to modify protein function through arginine methylation makes it a valuable tool for studying the role of this post-translational modification in different cellular processes.

One of the major applications of recombinant human PRMT1 protein is in the study of gene expression regulation. By methylating histone proteins, PRMT1 can influence the accessibility of DNA for transcription, thereby regulating gene expression. In addition, PRMT1 also methylates transcription factors and coactivators, which can affect their activity and lead to changes in gene expression.

Another important application of recombinant human PRMT1 protein is in the development of potential therapeutics. Dysregulation of PRMT1 has been implicated in various diseases, such as cancer, cardiovascular diseases, and neurodegenerative disorders. Therefore, targeting PRMT1 with specific inhibitors or activators could potentially lead to the development of novel treatments for these diseases.

Conclusion

In summary, recombinant human PRMT1 protein is a key enzyme involved in protein arginine methylation, which plays a critical role in regulating various cellular processes. Its structure, activity, and applications make it a valuable tool for understanding the role of protein arginine methylation in health and disease. Further research on this protein could potentially lead to the development of new therapeutic strategies for various diseases.