SmD3蛋白的对称二甲基精氨酸翻译后修饰对于小核核糖核蛋白（snRNP）的组装和核运输并非必需。
The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport.
作者信息
Khusial Permanan R, Vaidya Keta, Zieve Gary W
机构信息
Department of Pathology, Health Sciences Center, Stony Brook University, Stony Brook, NY 11794-8691, USA.
出版信息
Biochem Biophys Res Commun. 2005 Dec 2;337(4):1119-24. doi: 10.1016/j.bbrc.2005.09.161. Epub 2005 Oct 5.
The SmB, SmD1, and SmD3 proteins have the rare symmetrical dimethylarginine post-translational modification in their C-termini. In this report, we investigate the function of this modification in the assembly and intracellular transport of the SmD3 protein. We show that the elimination of this methylation in the SmD3 protein, by mutating the modified arginines to leucines, does not interfere with the assembly and the nuclear transport of the transiently expressed SmD3 variant. This suggests this modification is not essential for maturation of the SmD3 protein.
SmB、SmD1和SmD3蛋白在其C末端具有罕见的对称二甲基精氨酸翻译后修饰。在本报告中，我们研究了这种修饰在SmD3蛋白组装和细胞内运输中的功能。我们发现，通过将修饰的精氨酸突变为亮氨酸来消除SmD3蛋白中的这种甲基化，并不干扰瞬时表达的SmD3变体的组装和核运输。这表明这种修饰对于SmD3蛋白的成熟不是必需的。
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