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Article summary:
1. PRMT5 is an enzyme that catalyzes the symmetric dimethylation of arginine, which has distinct biological effects.
2. The structure of PRMT5 was analyzed and a conserved phenylalanine in the active site was found to be critical for specifying symmetric addition of methyl groups.
3. Changing this phenylalanine to a methionine significantly increases the overall methylase activity, but also converts PRMT5 to an enzyme that can catalyze both symmetric and asymmetric dimethylation of arginine.
Article analysis:
The article provides a detailed analysis of the structure of protein arginine methyltransferase 5 (PRMT5), an enzyme that catalyzes the symmetric dimethylation of arginine, and its implications for gene expression regulation. The article is well-written and provides clear evidence for its claims, including structural data from X-ray crystallography experiments and biochemical data from in vitro assays. The authors provide a comprehensive overview of the current understanding of PRMT5’s role in gene expression regulation, as well as its potential implications for other biological processes such as splicing regulation, circadian rhythms, DNA damage response, and germ cell development and pluripotency.
The article does not appear to have any major biases or unsupported claims; however, it does not explore any potential risks associated with manipulating PRMT5 activity or any counterarguments to its conclusions. Additionally, while the authors do discuss some potential applications for their findings (e.g., providing versatile control over eukaryotic gene expression), they do not provide any concrete examples or further discussion on how these findings could be applied in practice. Finally, while the authors do provide some background information on type-I arginine dimethylases (which add two methyl groups to the same ω-guanidino nitrogen atom), they do not discuss how these enzymes differ from PRMT5 in terms of their catalytic mechanisms or product specificity.