The nuclear import signal of snRNPs is composed of two essential components, the m(3)G cap structure of the snRNA and the Sm core NLS carried by the Sm protein core complex. We have previously proposed that, in yeast, this last determinant is represented by a basic-rich protuberance formed by the C-terminal extensions of Sm proteins. In mammals, as well as in other organisms, this component has not yet been precisely defined. Using GFP-Sm fusion constructs and immunolocalization as well as biochemical experiments, we show here that the C-terminal domains of human SmD1 and SmD3 proteins possess nuclear localization properties. Deletions of these domains increase cytoplasmic fluorescence and cytoplasmic localization of GFP-Sm mutant fusion alleles. Our results are consistent with a model in which the Sm core NLS is evolutionarily conserved and composed of a basic-rich protuberance formed by C-terminal domains of different Sm subtypes.
Nuclear localization properties of a conserved protuberance in the Sm core complex
Girard, C.; Mouaikel, J.; Neel, H.; Bertrand, E.; Bordonne, R.
Exp Cell Res
2004-09-10 / vol 299 / pages 199-208
IGMM team(s) involved in this publication
Assembly and Traffic of Ribonucleoproteins
Humans; Animals; Molecular Sequence Data; Evolution, Molecular; Autoantigens; Cytoplasm/genetics/metabolism; Recombinant Fusion Proteins/genetics/metabolism; Sequence Homology, Amino Acid; Phylogeny; Sequence Homology, Nucleic Acid; *Saccharomyces cerevisiae Proteins; Ribonucleoproteins, Small Nuclear/genetics/*metabolism; Cell Nucleus/*genetics/*metabolism; Macromolecular Substances; RNA, Small Nuclear/genetics/*metabolism; Active Transport, Cell Nucleus/genetics; Protein Structure, Tertiary/genetics