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Papers In Press, published online ahead of print December 26, 2001
J. Biol. Chem, 10.1074/jbc.M109984200
Submitted on October 16, 2001
Revised on December 26, 2001
Accepted on December 24, 2001

A novel WD repeat protein component of the methylosome binds Sm proteins

Westley J. Friesen, Anastasia Wyce, Sergey Paushkin, Linda Abel, Juri Rappsilber, Matthias Mann, and Gideon Dreyfuss

Department of Biochemistry-Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6148

Corresponding Author: gdreyfuss{at}hhmi.upenn.edu

We have recently described a large (20S) protein arginine methyltransferase complex, termed the methylosome, that contains the methyltransferase JBP1 (PRMT5) and the pICln protein. The methylosome functions to modify specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins, and this modification targets these proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein (snRNP) core particles. Here, we describe a novel component of the methylosome, a 50 kilodalton WD repeat protein termed methylosome protein 50 (MEP50). We show that MEP50 is important for methylosome activity and binds to JBP1 and to a subset of Sm proteins. Because WD repeat proteins provide a platform for multiple protein interactions, MEP50 may function to mediate the interaction of multiple substrates with the methylosome. Interestingly, all of the known components of the methylosome bind Sm proteins suggesting that in addition to producing properly methylated substrates for the SMN complex, the methylosome may be involved in Sm protein rearrangements or pre-assembly required for snRNP biogenesis.


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