Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity

Proper protein arginine methylation by protein arginine methyltransferase 1 (PRMT1) is critical for maintaining cellular health, while dysregulation is often associated with disease. How the activity of PRMT1 is regulated is therefore paramount, but is not clearly understood. Several studies have ob...

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Veröffentlicht in:	Protein science 2024-08, Vol.33 (8), p.e5118-n/a
Hauptverfasser:	Rossi, Vincent, Nielson, Sarah E., Ortolano, Ariana, Lonardo, Isabella, Haroldsen, Emeline, Comer, Drake, Price, Owen M, Wallace, Nathan, Hevel, Joan M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Arginine arginine methylation Cell lines Dimers effect of oligomerization on activity Electrophoresis enzyme oligomerization Humans Indigenous species Line spectra Methylation Monomers Oligomerization physiological concentrations Physiological effects Physiology Polyacrylamide PRMT1 Protein arginine methyltransferase protein methylation Protein Multimerization Protein-Arginine N-Methyltransferases - chemistry Protein-Arginine N-Methyltransferases - genetics Protein-Arginine N-Methyltransferases - metabolism Proteins regulation of PRMT1 activity Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism Substrate Specificity Substrates Western blotting
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