This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yao, K M Articles by White, K Search for Related Content PubMed PubMed Citation Articles by Yao, K M Articles by White, K

 Previous Article  |  Next Article 

Mol Cell Biol. 1991 June; 11(6): 2994-3000

Organizational analysis of elav gene and functional analysis of ELAV protein of Drosophila melanogaster and Drosophila virilis.

K M Yao and K White

Department of Biology, Brandeis University, Waltham, Massachusetts 02254-9110.

ABSTRACT

Drosophila virilis genomic DNA corresponding to the D. melanogaster embryonic lethal abnormal visual system (elav) locus was cloned. DNA sequence analysis of a 3.8-kb genomic piece allowed identification of (i) an open reading frame (ORF) with striking homology to the previously identified D. melanogaster ORF and (ii) conserved sequence elements of possible regulatory relevance within and flanking the second intron. Conceptual translation of the D. virilis ORF predicts a 519-amino-acid-long ribonucleoprotein consensus sequence-type protein. Similar to D. melanogaster ELAV protein, it contains three tandem RNA-binding domains and an alanine/glutamine-rich amino-terminal region. The sequence throughout the RNA-binding domains, comprising the carboxy-terminal 346 amino acids, shows an extraordinary 100% identity at the amino acid level, indicating a strong structural constraint for this functional domain. The amino-terminal region is 36 amino acids longer in D. virilis, and the conservation is 66%. In in vivo functional tests, the D. virilis ORF was indistinguishable from the D. melanogaster ORF. Furthermore, a D. melanogaster ORF encoding an ELAV protein with a 40-amino-acid deletion within the alanine/glutamine-rich region was also able to supply elav function in vivo. Thus, the divergence of the amino-terminal region of the ELAV protein reflects lowered functional constraint rather than species-specific functional specification.

---

Mol Cell Biol. 1991 June; 11(6): 2994-3000

This article has been cited by other articles:

• Toba, G., White, K. (2008). The third RNA recognition motif of Drosophila ELAV protein has a role in multimerization. Nucleic Acids Res 36: 1390-1399 [Abstract] [Full Text]  
• Soller, M., White, K. (2005). ELAV Multimerizes on Conserved AU4-6 Motifs Important for ewg Splicing Regulation. Mol. Cell. Biol. 25: 7580-7591 [Abstract] [Full Text]  
• Badciong, J. C., Otto, J. M., Waring, G. L. (2001). The Functions of the Multiproduct and Rapidly Evolving dec-1 Eggshell Gene Are Conserved Between Evolutionarily Distant Species of Drosophila. Genetics 159: 1089-1102 [Abstract] [Full Text]  
• Lisbin, M. J., Qiu, J., White, K. (2001). The neuron-specific RNA-binding protein ELAV regulates neuroglian alternative splicing in neurons and binds directly to its pre-mRNA. Genes Dev. 15: 2546-2561 [Abstract] [Full Text]  
• Lisbin, M. J., Gordon, M., Yannoni, Y. M., White, K. (2000). Function of RRM Domains of Drosophila melanogaster ELAV: RNP1 Mutations and RRM Domain Replacements With ELAV Family Proteins and SXL. Genetics 155: 1789-1798 [Abstract] [Full Text]  
• Yannoni, Y., White, K (1999). Domain necessary for Drosophila ELAV nuclear localization: function requires nuclear ELAV. J. Cell Sci. 112: 4501-4512 [Abstract]  
• Samson, M.-L. (1998). Evidence for 3' Untranslated Region-Dependent Autoregulation of the Drosophila Gene Encoding the Neuronal Nuclear RNA-Binding Protein ELAV. Genetics 150: 723-733 [Abstract] [Full Text]  
• Samson, M.-L. (2000). Drosophila Arginase Is Produced from a Nonvital Gene That Contains the elav Locus within Its Third Intron. J. Biol. Chem. 275: 31107-31114 [Abstract] [Full Text]