Effect of fluvastatin on colon tumor cells

Abstract

This chapter discusses substrate interactions of protein prenyltransferases. The posttranslational modification of proteins by isoprenoids facilitates protein–membrane and protein–protein interactions. This modification is common in a variety of proteins. It is estimated that as much as 0.5% of mammalian brain proteins are prenylated. Among the known prenylated proteins are most of the small guanosine triphosphate (GTP)-binding proteins, the γ subunits of trimeric G proteins, and nuclear lamins. Protein prenylation is likely to affect a wide variety of cellular functions. Prenylation of proteins is catalyzed by protein prenyltransferases. In the reaction a thioether bond is formed between the sulfhydryl group of a cysteine residue, located near the carboxy terminus of the acceptor protein, and either a 15-carbon farnesyl or a 20-carbon geranylgeranyl isoprenoid. The nature of the prenyl modification is highly dependent on the specificity of the prenyltransferases. The three protein prenyltransferases isolated are (1) farnesyltransferase (FTase), (2) geranylgeranyltransferase I (GGTase I), and (3) geranylgeranyltransferase II (GGTase II).The determination of farnesyl pyrophosphate binding assay using nonisolated enzyme-[3H] farnesyl pyrophosphate complex is described in the chapter.