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Abstract

Sulfation is a ubiquitous biochemical reaction that regulates various cellular and biological events in organisms. It is orchestrated by two classes of enzymes, which either add (sulfotransferases) or remove (sulfatases) a sulfonate group from a large variety of biomolecules and xenobiotic compounds. In nematodes, sulfation has been shown to control development and phenotypic plasticity, however, our understanding of the underlying mechanisms remains limited. Here, we investigate the role of the cytosolic sulfotransferases (SULTs) in Pristionchus pacificus (Ppa) which are expected to facilitate the sulfation of small compounds like hormones, bioamines and drugs, aiding in detoxification and hormonal metabolism. In contrast to Caenorhabditis and similarly in mammals, SULTs are expanded in the Pristionchus genus, with nine distinct enzymes encoded in its genome. To understand their biological role in Ppa, we executed a comprehensive analysis of expression and function of SULTs in worms. Using CRISPR-Cas9 genome editing, we built a collection of worms encoding a C-terminal Alfa tagged versions of the different SULTs and their corresponding null worms. In the meeting, we will present our high-resolution confocal microscopy experiments which show that SULTs expression is spatially restricted and indicates distinct functions for these enzymes in worms. Future work will aim at characterizing the role of these enzymes in worm biology.