Abstract
The Tudor domain is an approximately 60-amino acid structure motif in search of a function. Herein we show that the Tudor domains of the spinal muscular atrophy gene product SMN, the splicing factor 30 kDa (SPF30), and the Tudor domain-containing 3 (TDRD3) proteins interacted with arginine-glycine-rich motifs in a methylarginine-dependent manner. The Tudor domains also associated with methylarginine-containing cellular proteins, providing evidence that methylated arginines represent physiological ligands for this protein module. In addition, we report that spliceosomal small nuclear ribonucleoprotein particles core Sm proteins accumulated in the cytoplasm when arginine methylation was inhibited with adenosine dialdehyde or in the presence of an excessive amount of unmethylated arginine-glycine-rich peptides. These data provide in vivo evidence in support of a role for arginine methylation in the proper assembly and localization of spliceosomal Sm proteins.
Highlights
The Tudor domain is an ϳ60-amino acid structure motif in search of a function
We show that the Tudor domains of the spinal muscular atrophy gene product survival of motor neuron (SMN), the splicing factor 30 kDa (SPF30), and the Tudor domain-containing 3 (TDRD3) proteins interacted with arginine-glycine-rich motifs in a methylargininedependent manner
Tudor Domains Bind Endogenous Methylated Proteins—We generated a recombinant fusion protein consisting of glutathione S-transferase (GST) fused to amino acids 90 –149 of SMN encompassing the Tudor domain (GST-SMN-Tdr)
Summary
The Tudor domain is an ϳ60-amino acid structure motif in search of a function. we show that the Tudor domains of the spinal muscular atrophy gene product SMN, the splicing factor 30 kDa (SPF30), and the Tudor domain-containing 3 (TDRD3) proteins interacted with arginine-glycine-rich motifs in a methylargininedependent manner. The Tudor domains associated with methylarginine-containing cellular proteins, providing evidence that methylated arginines represent physiological ligands for this protein module. We report that spliceosomal small nuclear ribonucleoprotein particles core Sm proteins accumulated in the cytoplasm when arginine methylation was inhibited with adenosine dialdehyde or in the presence of an excessive amount of unmethylated arginine-glycine-rich peptides. These data provide in vivo evidence in support of a role for arginine methylation in the proper assembly and localization of spliceosomal Sm proteins. The Tudor domain mediates several of the interactions between SMN and its RG-containing binding partners [29, 42,43,44,45]
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