Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 2911K) PPT slides of all figures Supplemental Material Index Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Gonsalvez, G. B. Articles by Matera, A. G. Search for Related Content PubMed PubMed Citation Articles by Gonsalvez, G. B. Articles by Matera, A. G. Social Bookmarking                            What's this?

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

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.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

• Scoumanne, A., Zhang, J., Chen, X. (2009). PRMT5 is required for cell-cycle progression and p53 tumor suppressor function. Nucleic Acids Res 37: 4965-4976 [Abstract] [Full Text]  
• Fisk, J. C., Sayegh, J., Zurita-Lopez, C., Menon, S., Presnyak, V., Clarke, S. G., Read, L. K. (2009). A Type III Protein Arginine Methyltransferase from the Protozoan Parasite Trypanosoma brucei. J. Biol. Chem. 284: 11590-11600 [Abstract] [Full Text]  
• Patel, S. B., Bellini, M. (2008). The assembly of a spliceosomal small nuclear ribonucleoprotein particle. Nucleic Acids Res 36: 6482-6493 [Abstract] [Full Text]  
• Wang, L., Pal, S., Sif, S. (2008). Protein Arginine Methyltransferase 5 Suppresses the Transcription of the RB Family of Tumor Suppressors in Leukemia and Lymphoma Cells. Mol. Cell. Biol. 28: 6262-6277 [Abstract] [Full Text]  
• Kroiss, M., Schultz, J., Wiesner, J., Chari, A., Sickmann, A., Fischer, U. (2008). Evolution of an RNP assembly system: A minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 105: 10045-10050 [Abstract] [Full Text]  
• Gonsalvez, G. B., Praveen, K., Hicks, A. J., Tian, L., Matera, A. G. (2008). Sm protein methylation is dispensable for snRNP assembly in Drosophila melanogaster. RNA 14: 878-887 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents