The yolk proteins of Drosophila melanogaster comprise a family of three related yolk polypeptides each encoded by a single-copy gene. We show by genetic crosses that each gene makes an equivalent contribution to the fecundity and fertility of the female and they do not individually provide unique functions to the embryo. We show that the number of eggs laid by a female depends upon the number of genes encoding yolk polypeptides present in the genome and furthermore that the probability of an egg hatching into an adult also critically depends upon the number of yolk protein genes present in the mother. This suggests that the three yolk protein-encoding genes in Drosophila melanogaster may have arisen by duplication, then been maintained for quantitative reasons because they increased egg production and fertility, rather than each protein evolving a different function as is the case with most small gene families, such as tubulins and collagen genes.
The protein serine/threonine phosphatase 4 (PP4), which localises to centrosomes/spindle pole bodies in human cells, is shown to exhibit a similar localisation in Drosophila cells and embryos and possess a highly conserved (91% identical) amino acid sequence from humans to invertebrates. A homozygous Drosophila melanogaster strain mutant in the PP4 gene at 19C1-2 has been produced using P element mutagenesis. This strain, termed centrosomes minus microtubules (cmm), has reduced amounts of PP4 mRNA, approximately 25% of normal PP4 protein in early embryos and exhibits a semi-lethal phenotype with only 10% viability in certain conditions. Reversion mutagenesis shows that the phenotype is due to the presence of the P element in the PP4 mRNA. In early cmm embryos, nuclear divisions become asynchronous and large regions containing centrosomes with no well defined radiating microtubules are visible. In such areas, most nuclei arrest during mitosis with condensed DNA, and mitotic spindle microtubules are either absent, or aberrant and unconnected to the centrosome. A reduction in the staining of gamma-tubulin at centrosomes in cmm embryos suggests a conformational change or relocation of this protein, which is known to be essential for initiation of microtubule growth. These findings indicate that PP4 is required for nucleation, growth and/or stabilisation of microtubules at centrosomes/spindle pole bodies.
The l(1)su(f) mutation has been shown to suppress the developmentally regulated expression of glue protein genes at 30°C. Transferring mutant larvae to the restrictive temperature before the end of the second larval instar results in the absence or extreme reduction of glue protein synthesis while general protein synthesis is unaffected. At the same time, the three glue protein correlated chromosomal regions 3C, 25B, and 68C continue to show prominent puffs. The results suggest that the mutation may be affecting the processing or translatability of specific mRNAs rather than the translational machinery itself.
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