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Protein prenylation

The occurrence of protein prenylation in T. cruzi has been demonstrated.47 Protein prenylation in mammals and yeast involves the attachment of 15-carbon farnesyl or 20-carbon geranylgeranyl groups to a conserved cysteine residue in a CaaX motif of a subset of cellular proteins (Fig. 17.2). Many of these prenylated proteins are small GTPases, including Ras, Rac, Rab, and Rho, that have roles in cellular signal transduction and intracellular vesicle trafficking.66,67 The known functions of prenyl groups attached to cellular proteins is to anchor proteins to membranes and to serve as molecular handles for mediating protein—protein interactions.68 Three enzymes have been identified in eukaryotic cells including those from mammals and plants and in yeast that attach prenyl groups to proteins: protein farnesyl transferase (PFT); protein geranylgeranyl transferase I (PGGT-I); and protein geranylgeranyl transferase II (PGGT-II).68,69 Different studies have detected the presence of preny- lated proteins and a farnesyl transferase activity in T. cruzi.45—48 Over the past several years, hundreds of potent PFT inhibitors have been synthesized with the primary goal of developing anticancer drugs.70 Some of these compounds have been shown to inhibit the growth of T. cruzi47 and are potential chemotherapeutic agents.

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