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A more recent version of this article appeared on July 1, 2002
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Submitted on February 25, 2002
Revised on April 2, 2002
Accepted on April 12, 2002
1 Institut de Génétique Moléculaire, UMR5535 du CNRS, IFR 24, 1919 Route de Mende, F34293 Montpellier Cedex 5, France (present address: Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724)
2 Institut de Génétique Moléculaire, UMR5535 du CNRS, IFR 24, 1919 Route de Mende, F34293 Montpellier Cedex 5, France (present address: The Rockefeller University, 1230 York Avenue, New York, NY 10021-6399)
3 Institut de Génétique Moléculaire, UMR5535 du CNRS, IFR 24, 1919 Route de Mende, F34293 Montpellier Cedex 5, France
* Corresponding author. E-mail address: tazi{at}igm.cnrs-mop.fr.
Members of the highly conserved serine/arginine-rich protein (SR protein) family are nuclear factors involved in splicing of metazoan mRNA precursors. In mammals, two nuclear import receptors, transportin-SR1 (TRN-SR1) and transportin-SR2 (TRN-SR2), are responsible for targeting SR proteins to the nucleus. Distinctive features in the nuclear localization signal (NLS) between Drosophila and mammalian SR proteins prompted us to examine the mechanism by which Drosophila SR proteins and their antagonist repressor splicing factor 1 (RSF1) are imported into nucleus. Here, we report the identification and characterization of a Drosophila importin ß-family protein (dTRN-SR), homologous to TRN-SR2, that specifically interacts with both SR proteins and RSF1. dTRN-SR has a broad localization in the cytoplasm and the nucleus, whereas an N-terminal deletion mutant colocalizes with SR proteins in nuclear speckles. Far Western experiments established that the RS domain of SR proteins and the GRS domain of RSF1 are required for the direct interaction with dTRN-SR, an interaction that can be modulated by phosphorylation. Using the yeast model system in which nuclear import of Drosophila SR proteins and RSF1 is impaired, we demonstrate that complementation with dTRN-SR is sufficient to target these proteins to the nucleus. Altogether, the results imply that the mechanism by which SR proteins are imported to the nucleus is conserved between Drosophila and humans.
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