The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport.
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.
Khusial
Permanan R
PR
Department of Pathology, Health Sciences Center, Stony Brook University, Stony Brook, NY 11794-8691, USA.
Vaidya
Keta
K
Zieve
Gary W
GW
D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D001120:Arginine / Q000031:analogs & derivatives* / Q000378:metabolism; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D008745:Methylation; D008969:Molecular Sequence Data; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017411:Ribonucleoproteins, Small Nuclear / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D017411:Ribonucleoproteins, Small Nuclear; C487735:dimethylarginine; D001120:Arginine