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© The Rockefeller University Press, 0021-9525/1999//1145 $5.00
The Journal of Cell Biology, Volume 145, Number 6, , 1999 1145-1152

Transportin-SR, a Nuclear Import Receptor for SR Proteins

Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Department of Biochemistry and Biophysics, Philadelphia, Pennsylvania 19104-6148

The SR proteins, a group of abundant arginine/serine (RS)-rich proteins, are essential pre-mRNA splicing factors that are localized in the nucleus. The RS domain of these proteins serves as a nuclear localization signal. We found that RS domain–bearing proteins do not utilize any of the known nuclear import receptors and identified a novel nuclear import receptor specific for SR proteins. The SR protein import receptor, termed transportin-SR (TRN-SR), binds specifically and directly to the RS domains of ASF/SF2 and SC35 as well as several other SR proteins. The nuclear transport regulator RanGTP abolishes this interaction. Recombinant TRN-SR mediates nuclear import of RS domain– bearing proteins in vitro. TRN-SR has amino acid sequence similarity to several members of the importin β/transportin family. These findings strongly suggest that TRN-SR is a nuclear import receptor for the SR protein family.

Key Words: SR proteins • RS domain • nuclear localization signal • nuclear import receptor • RanGTP

Abbreviations used in this paper: GST, glutathione-S-transferase; hnRNP, heterogeneous nuclear RNP; IBB, importin β–binding domain; MBP, maltose-binding protein; NLS, nuclear localization signal; NPC, nuclear pore complex; RS domain, arginine/serine rich domain; TRN1, transportin 1; TRN-SR, transportin-SR.

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