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Nucleic Acids Research 2005 33(19):6372-6383; doi:10.1093/nar/gki942
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Published online 10 November 2005

Nucleic Acids Research, 2005, Vol. 33, No. 19 6372-6383
© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Shared RNA-binding sites for interacting members of the Drosophila ELAV family of neuronal proteins

Claudia D. Borgeson1 and Marie-Laure Samson1,2,*

1Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center Omaha, NE 68198-4525, USA 2Laboratoire Signalisation, Développement et Cancer, UMRC8080, CNRS, Université Paris Sud Bâtiment 442 bis, 91405 Orsay Cedex, France

*To whom correspondence should be addressed. Tel: +33 1 69 15 75 85; Fax: +33 1 69 15 68 03; Email: MLaure.Samson{at}ibaic.u-psud.fr

Received September 6, 2005. Revised October 17, 2005. Accepted October 17, 2005.

The product of the Drosophila embryonic lethal abnormal visual system is a conserved protein (ELAV) necessary for normal neuronal differentiation and maintenance. It possesses three RNA-binding domains and is involved in the regulation of RNA metabolism. The long elav 3'-untranslated region (3'-UTR) is necessary for autoregulation. We used RNA-binding assays and in vitro selection to identify the ELAV best binding site in the elav 3'-UTR. This site resembles ELAV-binding sites identified previously in heterologous targets, both for its nucleotide sequence and its significant affinity for ELAV (Kd 40 nM). This finding supports our model that elav autoregulation depends upon direct interaction between ELAV and elav RNA. We narrowed down the best binding site to a 20 nt long sequence A(U5)A(U3)G(U2)A(U6) in an alternative 3' exon. We propose and test a model in which the regulated use of this alternative 3' exon is involved in normal elav regulation. Found in NEurons (FNE), another neuronal RNA-binding protein paralogous to ELAV, also binds this site. These observations provide a molecular basis for the in vivo interactions reported previously between elav and fne.

Present address: Claudia D. Borgeson, The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Box 986805, Omaha, NE 69198-6805, USA

DDBJ/EMBL/GenBank accession nos.+

+DQ004736, DQ243913 and DQ243914


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