Insects encounter a vast repertoire of chemicals in their natural environment, which can signal positive stimuli like the presence of a food source, a potential mate, or a suitable oviposition site as well as negative stimuli such as competitors, predators, or toxic substances reflecting danger. The presence of specialized chemoreceptors like taste and olfactory receptors allows animals to detect chemicals at short and long distances and accordingly, trigger proper behaviors toward these stimuli. Since the first description of olfactory and taste receptors in Drosophila melanogaster 15 years ago, our knowledge on the identity, properties, and function of specific chemoreceptors has increased exponentially. In the last years, multidisciplinary approaches combining genetic tools with electrophysiological techniques, behavioral recording, evolutionary analysis, and chemical ecology studies are shedding light on our understanding on the ecological relevance of specific chemoreceptors for the survival of Drosophila in their natural environment. In this review we discuss the current knowledge on chemoreceptors of both the olfactory and taste systems of the fruitfly. We focus on the relevance of particular receptors for the detection of ecologically relevant cues such as pheromones, food sources, and toxic compounds, and we comment on the behavioral changes that the detection of these chemicals induce in the fly. In particular, we give an updated outlook of the chemical communication displayed during one of the most important behaviors for fly survival, the courtship behavior. Finally, the ecological relevance of specific chemicals can vary depending on the niche occupied by the individual. In that regard, in this review we also highlight the contrast between adult and larval systems and we propose that these differences could reflect distinctive requirements depending on the change of ecological niche occupied by Drosophila along its life cycle.
Genome sequences predict the presence of many 2-oxoglutarate (2OG)-dependent oxygenases of unknown biochemical and biological functions in Drosophila. Ribosomal protein hydroxylation is emerging as an important 2OG oxygenase catalyzed pathway, but its biological functions are unclear. We report investigations on the function of Sudestada1 (Sud1), a Drosophila ribosomal oxygenase. As with its human and yeast homologs, OGFOD1 and Tpa1p, respectively, we identified Sud1 to catalyze prolyl-hydroxylation of the small ribosomal subunit protein RPS23. Like OGFOD1, Sud1 catalyzes a single prolyl-hydroxylation of RPS23 in contrast to yeast Tpa1p, where Pro-64 dihydroxylation is observed. RNAi-mediated Sud1 knockdown hinders normal growth in different Drosophila tissues. Growth impairment originates from both reduction of cell size and diminution of the number of cells and correlates with impaired translation efficiency and activation of the unfolded protein response in the endoplasmic reticulum. This is accompanied by phosphorylation of eIF2α and concomitant formation of stress granules, as well as promotion of autophagy and apoptosis. These observations, together with those on enzyme homologs described in the companion articles, reveal conserved biochemical and biological roles for a widely distributed ribosomal oxygenase.fruit fly | ribosome | dioxygenase | proline | tranlational stress I ron [Fe(II)]-and 2-oxoglutarate (2OG)-dependent oxygenases are a superfamily with diverse biochemical and biological functions. During 2OG oxygenase catalysis, substrate oxidation is coupled to decarboxylation of 2OG, yielding succinate and carbon dioxide (1, 2). Structural studies reveal that the catalytic domain of 2OG oxygenases contains a conserved double-stranded β-helix (DSBH) fold presenting an HXD. . .H facial triad motif that coordinates an Fe(II) cofactor (3, 4). These and other structural features have been used to predict the existence of multiple uncharacterized 2OG oxygenases. In contrast to microorganisms and plants where 2OG oxygenases catalyze a wide variety of oxidative reactions, in animals their biochemical activities appear limited to hydroxylations or demethylations via hydroxylation (1,5,6). Despite progress in making biochemical assignments, the physiological roles of most 2OG oxygenases predicted by bioinformatic analysis of animal genomes are unknown. For instance, we have identified ∼50 putative 2OG oxygenases in the Drosophila genome, but only a few are characterized (7,8).The function of Fatiga, the single Drosophila homolog of human hypoxia inducible transcription factor (HIF) prolyl-4-hydroxylases (PHDs), has been well studied in the context of oxygen sensing (9). HIF prolyl-hydroxylation plays a central role in the animal hypoxic response via hydroxylation of HIF, a posttranslational modification that signals for HIF-α degradation in a physiologically relevant oxygen-dependent manner (10, 11). Given the tractability of these enzymes as targets for pharmacological modulation by 2OG analogs and related co...
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