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Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin

Kellie A. Dean^1,2,*, Oliver von Ahsen², Dirk Görlich² and Howard M. Fried^1,

¹ Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
² Zentrum für Molekulare Biologie der Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Federal Republic of Germany
^* Present address: Department of Genetics, Duke University Medical Center, Box 3657, Durham, NC 27710, USA

Author for correspondence (e-mail: refried{at}email.unc.edu)

Accepted June 18, 2001

The signal recognition particle (SRP) is a cytoplasmic RNA-protein complex that targets proteins to the rough endoplasmic reticulum. Although SRP functions in the cytoplasm, RNA microinjection and cDNA transfection experiments in animal cells, as well as genetic analyses in yeast, have indicated that SRP assembles in the nucleus. Nonetheless, the mechanisms responsible for nuclear-cytoplasmic transport of SRP RNA and SRP proteins are largely unknown. Here we show that the 19 kDa protein subunit of mammalian SRP, SRP19, was efficiently imported into the nucleus in vitro by two members of the importin ß superfamily of transport receptors, importin 8 and transportin; SRP19 was also imported less efficiently by several other members of the importin ß family. Although transportin is known to import a variety of proteins, SRP19 import is the first function assigned to importin 8. Furthermore, we show that a significant pool of endogenous SRP19 is located in the nucleus, as well as the nucleolus. Our results show that at least one mammalian SRP protein is specifically imported into the nucleus, by members of the importin ß family of transport receptors, and the findings add additional evidence for nuclear assembly of SRP.

Key words: Importin, Nuclear transport, Nucleolus, Signal recognition particle, SRP19

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