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PubMed1990

Viability of first and second generation hybrids of Drosophila virilis and Drosophila lummei.

F1 hybrids of D. virilis and D. lummei survived significantly worse than the parents. When D. virilis was the mother, larger proportion of hybrids failed to emerge from pupal case, but overall survival rate of reciprocals was about the same. Viability of different heterospecific combinations of sex chromosomes and autosomes was studied in backcrosses. All the sex chromosomes survived well on the background of all-heterozygous autosomes. Hemizygous X was reciprocally subvital with homozygous alien autosomes. The reduced viability was male sex limited. The X-linked factor causing this effect was localized in the area of the large, phylogenetically ancient double inversion In(1)a+b. All four large autosomes were heterotic in backcross hybrids, more strongly in females. Five out of six possible first degree interactions between the autosomes were negative, indicating incompatibility between heterospecific autosomes. This effect was stronger in females. The genetic basis for hybrid subvitality is sex-specific.

Animals↗
PubMed2006

Expression of a functional Drosophila melanogaster CMP-sialic acid synthetase. Differential localization of the Drosophila and human enzymes.

CMP-N-acetylneuraminic acid is a critical metabolite in the generation of glycoconjugates that play a role in development and other physiological processes. Whereas pathways for its generation are firmly established in vertebrates, the presence and function of the relevant synthetic enzyme in insects and other protostomes is unknown. In this study, we characterize the first functional CMP-sialic acid synthase (DmCSAS) from any protostome lineage expressed from a D. melanogaster cDNA clone. Homologous genes were subsequently identified in other insect species. The gene is developmentally regulated, with expression first appearing at 12-24 h of embryogenesis, low expression through larval and pupal stages, and greatly enriched expression in the adult head, suggesting a possible role in the central nervous system. Activity of the enzyme was verified by an increase in in vitro and in vivo CMP-N-acetylneuraminic acid levels when expressed in a heterologous host. Unlike all known vertebrate CMP-sialic acid synthetase (CSAS) proteins that localize to the nucleus, the D. melanogaster CSAS protein was targeted to the Golgi compartment when expressed in both heterologous mammalian and insect cell lines. Replacement of the N-terminal leader sequence of DmCSAS with the human CSAS N-terminal sequence resulted in the redirection of the chimeric CSAS protein to the nucleus but with a concomitant loss of enzymatic activity. The localization of CSAS orthologs to different intracellular organelles represents, to our knowledge, the first example of differential protein targeting of orthologs in eukaryotes and reveals how the sialylation pathway diverged during the evolution of protostomes and deuterostomes.

Amino Acid Sequence↗