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Molecular and Cellular Biology, February 2001, p. 1345-1359, Vol. 21, No. 4
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.4.1345-1359.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Distinctive Features of Drosophila Alternative Splicing Factor RS Domain: Implication for Specific Phosphorylation, Shuttling, and Splicing Activation

Eric Allemand,1 Renata Gattoni,2 Henri-Marc Bourbon,3 James Stevenin,2 Javier F. Cáceres,4 Johann Soret,1 and Jamal Tazi1,*

Institut de Génétique Moléculaire, UMR5535 du CNRS, IFR 24, F34293 Montpellier Cedex 5,1 Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, C. U. de Strasbourg,2 and Centre de Biologie du Développement, UMR5547 du CNRS, Université Paul Sabatier, Toulouse,3 France, and MRC Human Genetics Unit, Edinburgh, United Kingdom4

Received 20 September 2000/Returned for modification 5 November 2000/Accepted 9 November 2000

The human splicing factor 2, also called human alternative splicing factor (hASF), is the prototype of the highly conserved SR protein family involved in constitutive and regulated splicing of metazoan mRNA precursors. Here we report that the Drosophila homologue of hASF (dASF) lacks eight repeating arginine-serine dipeptides at its carboxyl-terminal region (RS domain), previously shown to be important for both localization and splicing activity of hASF. While this difference has no effect on dASF localization, it impedes its capacity to shuttle between the nucleus and cytoplasm and abolishes its phosphorylation by SR protein kinase 1 (SRPK1). dASF also has an altered splicing activity. While being competent for the regulation of 5' alternative splice site choice and activation of specific splicing enhancers, dASF fails to complement S100-cytoplasmic splicing-deficient extracts. Moreover, targeted overexpression of dASF in transgenic flies leads to higher deleterious developmental defects than hASF overexpression, supporting the notion that the distinctive structural features at the RS domain between the two proteins are likely to be functionally relevant in vivo.

* Corresponding author. Mailing address: Institut de Génétique Moléculaire, UMR5535 du CNRS, IFR 24, 1919 Route de Mende, F34293 Montpellier Cedex 5, France. Phone: (33) 04 67 61 36 85. Fax: (33) 04 67 04 02 45. E-mail: tazi{at}igm.cnrs-mop.fr.

Molecular and Cellular Biology, February 2001, p. 1345-1359, Vol. 21, No. 4
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.4.1345-1359.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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