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Nucleic Acids Research Advance Access published online on January 18, 2008
Nucleic Acids Research, doi:10.1093/nar/gkm1168
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

The third RNA recognition motif of Drosophila ELAV protein has a role in multimerization

Gakuta Toba* and Kalpana White

Department of Biology and Volen National Center for Complex Systems, MS008, Brandeis University, Waltham, Massachusetts 02454, USA

*To whom correspondence should be addressed. Tel: +81-22-795-5790; Fax: +81-22-795-7732; Email: gtoba{at}mail.tains.tohoku.ac.jp

Received August 16, 2007. Revised December 19, 2007. Accepted December 19, 2007.

ELAV is a neuron-specific RNA-binding protein in Drosophila that is required for development and maintenance of neurons. ELAV regulates alternative splicing of Neuroglian and erect wing (ewg) transcripts, and has been shown to form a multimeric complex on the last ewg intron. The protein has three RNA recognition motifs (RRM1, 2 and 3) with a hinge region between RRM2 and 3. In this study, we used the yeast two-hybrid system to determine the multimerization domain of ELAV. Using deletion constructs, we mapped an interaction activity to a region containing most of RRM3. We found three conserved short sequences in RRM3 that were essential for the interaction, and also sufficient to give the interaction activity to RRM2 when introduced into it. In our in vivo functional assay, a mutation in one of the three sequences showed reduced activity in splicing regulation, underlining the functional importance of multimerization. However, RRM2 with the three RRM3 interaction sequences did not function as RRM3 in vivo, which suggested that multimerization is not the only function of RRM3. Our results are consistent with a model in which RRM3 serves as a bi-functional domain that interacts with both RNA and protein.

Present address: Gakuta Toba, Graduate School of Life Sciences, Tohoku University, Aoba-ku, Sendai, Miyagi 980-8578, Japan


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