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Glycosylation and sulfation are two of the essential post-translational modifications of proteins. The slalom gene encodes a 3'-phosphoadenosine 5'-phosphosulfate transporter, a conserved protein found in organisms as diverse as plants and humans and required for sulfation of proteins. In Drosophila, slalom is exclusively expressed in salivary glands, which is unexpected, taken into account the general function for sulfation of proteins. In this paper, we present a detailed description of the slalom gene in a large insect, the blowfly Lucilia sericata. Our data demonstrate that the slalom gene structure, the protein and the expression pattern are highly conserved between Lucilia and Drosophila. Lucilia slalom promoter analysis, using transgenic Drosophila, demonstrates that the Lucilia slalom promoter can faithfully mimic the expression pattern of both Lucilia and Drosophila slalom in salivary glands. Taken together, these data show the structure and the transcriptional cis-regulatory elements of the slalom gene to be unchanged during evolution, despite the 100 million years of divergence between the two insects. Moreover, it suggests that the salivary gland-specific expression of slalom bears an important and conserved function for sulfation of specific macromolecules.

Structural conservation of the salivary gland-specific slalom gene in the blowfly Lucilia sericata