Ontology highlight
ABSTRACT:
SUBMITTER: Feng Y
PROVIDER: S-EPMC3873558 | biostudies-literature | 2013 Dec
REPOSITORIES: biostudies-literature
Feng You Y Maity Ranjan R Whitelegge Julian P JP Hadjikyriacou Andrea A Li Ziwei Z Zurita-Lopez Cecilia C Al-Hadid Qais Q Clark Amander T AT Bedford Mark T MT Masson Jean-Yves JY Clarke Steven G SG
The Journal of biological chemistry 20131118 52
The mammalian protein arginine methyltransferase 7 (PRMT7) has been implicated in roles of transcriptional regulation, DNA damage repair, RNA splicing, cell differentiation, and metastasis. However, the type of reaction that it catalyzes and its substrate specificity remain controversial. In this study, we purified a recombinant mouse PRMT7 expressed in insect cells that demonstrates a robust methyltransferase activity. Using a variety of substrates, we demonstrate that the enzyme only catalyzes ...[more]