화학공학소재연구정보센터
Biochemical and Biophysical Research Communications, Vol.337, No.4, 1119-1124, 2005
The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport
The SinB, 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. (c) 2005 Elsevier Inc. All rights reserved.