Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins

Graydon B. Gonsalvez (Lead / Corresponding author), Liping Tian, Jason K. Ospina, François Michel Boisvert, Angus I. Lamond, A. Gregory Matera

    Research output: Contribution to journalArticle

    101 Citations (Scopus)

    Abstract

    Small nuclear ribonucleoproteins (snRNPs) are core components of the spliceosome. The U1, U2, U4, and U5 snRNPs each contain a common set of seven Sm proteins. Three of these Sm proteins are posttranslationally modified to contain symmetric dimethylarginine (sDMA) residues within their C-terminal tails. However, the precise function of this modification in the snRNP biogenesis pathway is unclear. Several lines of evidence suggest that the methyltransferase protein arginine methyltransferase 5 (PRMT5) is responsible for sDMA modification of Sm proteins. We found that in human cells, PRMT5 and a newly discovered type II methyltransferase, PRMT7, are each required for Sm protein sDMA modification. Furthermore, we show that the two enzymes function nonredundantly in Sm protein methylation. Lastly, we provide in vivo evidence demonstrating that Sm protein sDMA modification is required for snRNP biogenesis in human cells.

    Original languageEnglish
    Pages (from-to)733-740
    Number of pages8
    JournalJournal of Cell Biology
    Volume178
    Issue number5
    DOIs
    Publication statusPublished - 27 Aug 2007

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