Ontology highlight
ABSTRACT:
SUBMITTER: Kolbel K
PROVIDER: S-EPMC2659185 | biostudies-other | 2009 Mar
REPOSITORIES: biostudies-other
Kölbel Knut K Ihling Christian C Bellmann-Sickert Kathrin K Neundorf Ines I Beck-Sickinger Annette G AG Sinz Andrea A Kühn Uwe U Wahle Elmar E
The Journal of biological chemistry 20090121 13
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 ...[more]