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Published online August 20, 2007
doi:10.1083/jcb.200702147
The Journal of Cell Biology, Vol. 178, No. 5, 733-740
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Gonsalvez et al.
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 Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins

Graydon B. Gonsalvez1, Liping Tian1, Jason K. Ospina1, François-Michel Boisvert2, Angus I. Lamond2, and A. Gregory Matera1

1 Department of Genetics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106
2 School of Life Sciences, Wellcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, Scotland, UK

Correspondence to Graydon B. Gonsalvez: gbg3{at}cwru.edu

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.

Abbreviations used in this paper: aDMA, asymmetric dimethylarginine; CB, Cajal body; MTA, 5'-deoxy-5'-(methylthio)adenosine; PRMT, protein arginine methyltransferase; sDMA, symmetric dimethylarginine; SMN, survival of motor neurons; snRNA, small nuclear RNA; snRNP, small nuclear RNP; TMG, trimethylguanosine.


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