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Details on Person Protein arginine N-methyltransferase 1 (PRMT1) transfers the...
| Class:Id | Summation:9759646 |
|---|---|
| _displayName | Protein arginine N-methyltransferase 1 (PRMT1) transfers the... |
| _timestamp | 2021-12-10 17:44:33 |
| created | [InstanceEdit:9759655] Shamovsky, Veronica, 2021-12-10 |
| literatureReference | [LiteratureReference:9759649] Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding [LiteratureReference:9759658] Molecular Mechanism underlying PRMT1 Dimerization for SAM Binding and Methylase Activity [LiteratureReference:9759671] Naturally occurring cancer-associated mutations disrupt oligomerization and activity of protein arginine methyltransferase 1 (PRMT1) [LiteratureReference:9759674] Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides [LiteratureReference:9759667] Understanding protein arginine methyltransferase 1 (PRMT1) product specificity from molecular dynamics [LiteratureReference:9759685] Structure, Activity, and Function of PRMT1 [LiteratureReference:9759694] Transient Kinetics Define a Complete Kinetic Model for Protein Arginine Methyltransferase 1 [LiteratureReference:9759700] Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively [LiteratureReference:9759691] Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism [LiteratureReference:9759699] Activity-based protein profiling of protein arginine methyltransferase 1 [LiteratureReference:9759693] Kinetic mechanism of protein arginine methyltransferase 1 |
| modified | [InstanceEdit:9759698] Shamovsky, Veronica, 2021-12-10 |
| text | Protein arginine N-methyltransferase 1 (PRMT1) transfers the methyl group from S-adenosyl-L-methionine (SAM, also known as AdoMet) to the side-chain nitrogens of arginine residues, forming omega-mono- or asymmetric dimethylarginine on both chromatin-bound and cytoplasmic proteins and S-adenosyl-L-homocysteine (SAH, also known as AdoHcy) (Gathiaka S et al. 2016; reviewed in Thiebaut C et al. 2021). Kinetic analysis suggests that PRMT1-medated dimethylation of its substrates proceeds in a distributive manner (Kölbel K et al. 2009; Hu H et al. 2016). However, several studies support a semi-processive mechanisms for PRMT1 activity (Obianyo O et al. 2008; 2011). The degree of enzyme processivity depended on substrate sequence, cofactor or enzyme concentrations (Brown JI et al. 2018). Molecular dynamics simulations data suggest that PRMT1 forms dimers (Zhou R et al. 2015). The dimer inteface is formed between the dimerization arm of one monomer and AdoMet binding site in the the N-terminus of another monomer leading to conformational fluctuations in the N terminus. A combination of computational methods, site-directed mutagenesis, native PAGE, and enzymatic activity assays in vitro suggests that the dimer conformation of PRMT1 facilitates AdoMet binding and methyltransferase activity of PRMT1 (Zhou R et al. 2015). Structural studies showed that dimerization of rat ortholog of human PRMT1 is essential for PRMT1 enzymatic activity (Zhang X & Cheng X 2003). Further, naturally occurring cancer-associated mutations in the dimerization arm of human PRMT1 disrupt its self-association and alter methyltransferase activity (Price OM et al. 2021). PRMT1 methylates cellular nucleic acid binding protein (CNBP) in the RG-rich sequence between the first and the second zinc finger repeats forming asymmetric dimethylarginines at R25 and R27 (Wei HM et al. 2014). This methylation event impaired RNA binding activity of CNBP, but did not affect its subcellular localization (Wei HM et al. 2014). |
| (summation) | [Reaction:9759652] PRMT1 transfers 3xCH3 from 3xAdoMet to CNBP [Homo sapiens] |
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