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Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively*S⃞

By Knut Kölbel, Christian Ihling, Kathrin Bellmann-Sickert, Ines Neundorf, Annette G. Beck-Sickinger, Andrea Sinz, Uwe Kühn and Elmar Wahle

Abstract

Asymmetric dimethylation of arginine residues is a common posttranslational modification of proteins carried out by type I protein arginine methyltransferases, including PRMT1 and -3. We report that the consecutive transfer of two methyl groups to a single arginine side chain by PRMT1 and -3 occurs in a distributive manner, i.e. with intermittent release of the monomethylated intermediate. The oligomeric state of PRMTs together with the clustering of methylated arginine residues in most proteins carrying this type of modification suggests that multiple methyl transfers to a single polypeptide chain might proceed in a processive manner by cooperation of multiple active sites. However, three different types of experiments provide evidence that the reaction is distributive even with substrates containing multiple methyl-accepting arginines, including one with 13 such residues. PRMT1 also does not prefer substrates already containing one or more singly or doubly methylated arginine residues. Even though the reaction is distributive, the efficiency of methylation of one particular protein strongly depends on the number of methyl-accepting arginine residues it contains

Topics: Protein Synthesis, Post-Translational Modification, and Degradation
Publisher: American Society for Biochemistry and Molecular Biology
OAI identifier: oai:pubmedcentral.nih.gov:2659185
Provided by: PubMed Central
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