Methylation of Histone H3 by Coactivator-Associated Arginine Methyltransferase 1†
作者： Brandon T. Schurter , Stephen S. Koh , Dagang Chen , Gerard J. Bunick , Joel M. Harp
DOI: 10.1021/BI002631B
关键词:
摘要: The preferential in vitro methylation of histone H3 by coactivator-associated arginine methyltransferase 1 (CARM1) has been proposed as a basis for its ability to enhance gene transcription [Chen, D., et al. (1999) Science 284, 2174−2177]. To further evaluate the significance methylation, we studied kinetics and site specificity modification CARM1. Affinity-purified CARM1 methylated recombinant chick H3, which is free posttranslational modifications, calf thymus heterogeneous with regard preexisting equally well, exhibiting Vmax 4500 pmol min-1 (mg enzyme)-1 an apparent Km ≤0.2 μM. catalytic efficiency (kcat/Km) toward was at least 1000 times that R1 (GGFGGRGGFGG-amide), highly effective substrate protein 1. Peptide mapping 3H-methyl-labeled indicated Arg-2, Arg-17, Arg-26 N-terminal region one or more four arginines (128/129/131/...
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