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Genetics, Vol 141, 1101-1111, Copyright © 1995
INVESTIGATIONS |
Two Distinct Temperature-Sensitive Alleles at the elav Locus of Drosophila Are Suppressed Nonsense Mutations of the Same Tryptophan Codon
M. L. Samson, M. J. Lisbin and K. White
Waksman Institute, Rutgers, The State University, Piscataway, New Jersey 08855, and Department of Biology and Volen National Center for Complex Systems, Brandeis University, Waltham, Massachusetts 02254 Present address: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198.
The Drosophila gene elav encodes a 483-amino-acid-long nuclear RNA binding protein required for normal neuronal differentiation and maintenance. We molecularly analyzed the three known viable alleles of the gene, namely elav(ts1), elav(FliJ1), and elav(FliJ2), which manifest temperature-sensitive phenotypes. The modification of the elav(FliJ1) allele corresponds to the change of glycine(426) (GGA) into a glutamic acid (GAA). Surprisingly, elav(ts1) and elav(FliJ2) were both found to have tryptophan(419) (TGG) changed into two different stop codons, TAG and TGA, respectively. Unexpectedly, protein analysis from elav(ts1) and elav(FliJ2) reveals not only the predicted 45-kD truncated ELAV protein due to translational truncation, but also a predominant full-size 50-kD ELAV protein, both at permissive and nonpermissive temperatures. The full-length protein present in elav(ts1) and elav(FliJ2) can a priori be explained by one of several mechanisms leading to functional suppression of the nonsense mutation or by detection of a previously unrecognized ELAV isoform of similar size resulting from alternative splicing and unaffected by the stop codon. Experiments described in this article support the functional suppression of the nonsense mutation as the mechanism responsible for the full-length protein.
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