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Vol. 13, Issue 7, 2436-2447, July 2002

A Conserved Drosophila Transportin-Serine/Arginine-rich (SR) Protein Permits Nuclear Import of Drosophila SR Protein Splicing Factors and Their Antagonist Repressor Splicing Factor 1

Eric Allemand,^* Svetlana Dokudovskaya,^* Rémy Bordonné, and Jamal Tazi^§

Institut de Génétique Moléculaire, Unité Mixte Recherche 5535 du Centre National de la Recherche Scientifique, l'Institut Fédératif de Recherches 24, F34293 Montpellier, France

Members of the highly conserved serine/arginine-rich (SR) protein family are nuclear factors involved in splicing of metazoan mRNA precursors. In mammals, two nuclear import receptors, transportin (TRN)-SR1 and TRN-SR2, are responsible for targeting SR proteins to the nucleus. Distinctive features in the nuclear localization signal 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. Herein, we report the identification and characterization of a Drosophila importin -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. Together, 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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^* These authors contributed equally to this work.

Present addresses: Cold Spring Harbor Laboratory, 1 Bungtown Rd., Cold Spring Harbor, NY 11724; The Rockefeller University, 1230 York Ave., New York, NY 10021-6399.

^§ Corresponding author. E-mail address: tazi{at}igm.cnrs-mop.fr.

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Molecular Biology of the Cell
Vol. 13, 2436-2447, July 2002
Copyright © 2002 by The American Society for Cell Biology

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