Kafkova L, Debler EW, Fisk JC, Jain K, Clarke SG, and Read LK. The major protein arginine methyltransferase in T. brucei functions as an enzyme-prozyme complex. J. Biol. Chem., 292:2089, 2017

The major trypanosome protein arginine methyltransferase functions as an enzyme-prozyme pair, being the first example of a heteromeric PRMT and suggesting that enzyme-prozyme organization may be expanded in trypanosomes as a means of enzyme regulation.

Jain K, Warmack RA, Debler EW, Hadjikyriacou A, Stavropoulos P, and Clarke SG. Protein Arginine Methyltransferase Product Specificity is Mediated by Distinct Active-Site Architectures. J. Biol. Chem., 291:18299, 2016

We converted a protein arginine methyltransferase, which only produces monomethylarginine, into enzymes capable of asymmetric and symmetric dimethylarginine formation, providing a structural basis and a general model for product specificity in PRMTs.

Debler EW, Jain K, Warmack RA, Feng Y, Clarke SG, Blobel G, and Stavropoulos P. A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase. Proc. Natl. Acad. Sci. USA, 113:2068, 2016

Structural and biochemical analyses of a protein arginine monomethyltransferase provide insights into the mechanism of action and the exquisite product specificity of this important class of enzymes, linked to a variety of diseases.