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Published online 4 June 2004

Nucleic Acids Research, 2004, Vol. 32, No. 10 3070-3082
© 2004 Oxford University Press

The Drosophila Bruno paralogue Bru-3 specifically binds the EDEN translational repression element

Jérôme Delaunay, Gwenn Le Mée, Nader Ezzeddine, Gilles Labesse1, Christophe Terzian2, Michèle Capri and Ounissa Aït-Ahmed*

Institut de Génétique Humaine, UPR 1142 CNRS, 141 Rue de la Cardonille, 34396 Montpellier Cedex 5, France 1 Centre de Biochimie Structurale, 15 Avenue Charles Flahaut, 34060 Montpellier Cedex, France and 2 Ecole Pratique des Hautes Etudes, UMR 7625, Université Pierre et Marie Curie, 7 Quai Saint Bernard, 75252 Paris Cedex 5, France

*To whom correspondence should be addressed. Tel: +33 499 61 99 11; Fax: +33 499 61 99 01; Email: ounissa.ait-ahmed{at}igh.cnrs.fr
Present address:
Nader Ezzeddine, Department of Medicine, Albert Einstein College of Medicine, Forchheimer G46, 1300 Morris Park Avenue, Bronx, NY 10461, USA

Received March 9, 2004; Revised April 26, 2004;; Accepted May 10, 2004

We reported in our previous work that the EDEN-dependent translational repression of maternal mRNAs was conserved between Drosophila and Xenopus. In Xenopus, this repression is achieved through the binding of EDEN to the Bruno-like factor, EDEN-BP. We show in the present work that the Drosophila Bruno paralogue, the 45 kDa Bru-3 protein (p45), binds specifically to the EDEN element and acts as a homodimer. We describe for the first time a previously undetected 67 amino acid domain, found in the divergent linker region, the lsm domain (lsm stands for linker-specific motif). We propose that the presence of this domain in a subset of the Bruno-like proteins, including Bru-3, EDEN-BP and CUG-BP but not Bruno nor its other paralogue Bru-2, might be responsible for specific RNA recognition. Interestingly, comparative structural analyses using threaders and molecular modelling suggest that the new domain might be distantly related to the first RNA recognition motif of the Drosophila sex-lethal protein (sxl). The phylogenetic analyses and the experimental data based on its specific binding to the EDEN element support the conclusion that Bru-3 is an EDEN-BP/CUG-BP orthologue.


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