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A more recent version of this article appeared on December 6, 2002
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M204551200v1
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Papers In Press, published online ahead of print September 19, 2002
J. Biol. Chem, 10.1074/jbc.M204551200
Submitted on May 9, 2002
Revised on September 19, 2002
Accepted on September 19, 2002

Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified Box H/ACA snoRNP protein GAR1

Sarah E. Whitehead, Kevin W. Jones, Xing Zhang, Xiaodong Cheng, Rebecca M. Terns, and Michael P. Terns

Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602

Corresponding Author: mterns{at}bmb.uga.edu

Deletion or mutation of the SMN1 (survival of motor neurons) gene causes the common, fatal neuromuscular disease spinal muscular atrophy. The SMN protein is important in small nuclear (sn)RNP assembly and interacts with snRNP proteins via arginine/glycine-rich domains. Recently, SMN was also found to interact with core protein components of the two major families of small nucleolar (sno)RNPs, fibrillarin and GAR1, suggesting that SMN may also function in the assembly of snoRNPs. Here we present results that indicate that the interaction of SMN with GAR1 is mediated by the Tudor domain of SMN. Single point mutations within the Tudor domain, including an SMA patient mutation, impair the interaction of SMN with GAR1. Furthermore, we find that either of the two arginine/glycine-rich domains of GAR1 can provide for interaction with SMN, but removal of both results in loss of the interaction. Finally, we have found that unlike the interaction of SMN with the Sm snRNP proteins, interaction with GAR1 and fibrillarin is not enhanced by arginine dimethylation. Our results argue against post-translational arginine dimethylation as a general requirement for SMN recognition of proteins bearing arginine/glycine-rich domains.


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