Two distinct temperature-sensitive alleles at the elav locus of Drosophila are suppressed nonsense mutations of the same tryptophan codon

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 elavts1, elavFliJ1 and elavFliJ2 which manifest temperature-sensitive phenotypes...

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Bibliographic Details
Published in:Genetics (Austin) 1995-11, Vol.141 (3), p.1101-1111
Main Authors: Samson, M.L. (University of Nebraska Medical Center, Omaha, NE.), Lisbin, M.J, White, K
Format: Article
Language:English
Subjects:
Alleles
Amino Acid Sequence
Animals
Base Sequence
CODE GENETIQUE
CODIGO GENETICO
Codon - genetics
DROSOPHILA MELANOGASTER
Drosophila melanogaster - genetics
ELAV Proteins
Female
FENOTIPOS
GENE
GENES
Genes, Insect
Insects
Investigations
LOCI
LOCUS
Male
Molecular Sequence Data
MUTACION
MUTANT
MUTANTES
MUTATION
Neurons
PHENOTYPE
Point Mutation
Protein Biosynthesis
PROTEINAS AGLUTINANTES
PROTEINE DE LIAISON
Proteins
Ribonucleoproteins - biosynthesis
Ribonucleoproteins - genetics
RNA, Messenger - genetics
Suppression, Genetic
TEMPERATURA
TEMPERATURE
Terminator Regions, Genetic - genetics
Tryptophan
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Description
Summary: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 elavts1, elavFliJ1 and elavFliJ2 which manifest temperature-sensitive phenotypes. The modification of the elavFliJ2 allele corresponds to the change of glycine426 (GGA) into a glutamic acid (GAA). Surprisingly, elavFliJ2 and elavFliJ2 were both found to have tryptophan419 (TOG) changed into two different stop codons, TAG and TGA, respectively. Unexpectedly, protein analysis from elavts1 and elavFliJ2 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 elavts1 and elavFliJ2 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
ISSN:0016-6731
1943-2631
1943-2631
DOI:10.1093/genetics/141.3.1101