Worm Breeder's Gazette 14(1): 83 (October 1, 1995)
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
Dept. of Microbiology, Duke University Medical Center, Durham NC, 27710.
ELAV is a Drosophila protein that has been linked genetically to the differentiation of neuroblasts to neurons and is also responsible for the maintenance of terminally differentiated neurons. ELAV like proteins contain three RNA Recognition Motifs (RRMs), the first two RRMs are usually found at the N terminus of the protein separated by one or two amino acids. The third RRM is separated from the first two by a variable hinge region that appears to be alternatively spliced with the presence of miniexons that may influence the function of the protein. Several labs have successfully cloned homologs of the ELAV protein from other organisms such as rat, humans, and Xenopus. The human counterparts of ELAV have been shown to bind to AU rich stretches in the 3' untranslated regions of certain mRNAs, such as c-myc, c-fos, and gm-csf. Analysis of the Xenopus clones have shown that three of the ELAV homologs are expressed sequentially during the development of the frog embryo. While screening libraries for a C. elegans counterpart of ELAV, we found a cDNA that encoded a putative ORF encoding the first ELAV homolog. This clone corresponded to a predicted polypeptide on chromosome II sequenced by the genome sequencing project. Our screening has produced a full length clone corresponding to the predicted nucleotide sequence of the putative ORF. A western was performed using anti Human ELAV-Like Neuronal protein 1 (HEL-N1) rabbit polyclonal antisera against a protein extract of a mixed population of N2 worms and revealed a band, of the predicted size of the CEL-1 protein. Among other things we intend to determine the developmental regulation of this protein, attempt to rescue preexisting mutants, generate mutants if none now exist, determine the localization of the protein, elucidate the in vivo mRNA targets of the protein, and use the genetics of C. elegans to uncover the mechanism of action of this family of proteins.