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• W1492777072 abstract "This chapter describes various rationales for mutating a prenylation signal sequence and discusses the methodology for such mutation and for analyzing the success of the procedure. Different classes of prenylation signals are recognized by different prenyltransferases; signal sequences also contain recognition motifs for other posttranslational modifications, including proteolytic cleavage and carboxylmethylation. Proteins that are modified by prenylation include members of the ras superfamily of small (GTPases), γ subunits of heterotrimeric G proteins, nuclear lamins, retinal signal transducing proteins, yeast transport proteins and mating pheromones, and viral proteins required for virion assembly. It is sometimes desirable to mutate the prenylation motif of a protein to remove or alter the type of isoprenoid attached to it. Mutational analysis can complement genetic, pharmacological, and biochemical approaches to studying prenylation processes. The functional requirement for prenylation in the biological activity of prenylated proteins is because of the crucial role of prenylation in mediating protein–protein and protein–membrane interactions." @default.
• W1492777072 created "2016-06-24" @default.
• W1492777072 creator A5005839868 @default.
• W1492777072 date "1995-01-01" @default.
• W1492777072 modified "2023-10-10" @default.
• W1492777072 title "[10] Mutation and analysis of prenylation signal sequences" @default.
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• W1492777072 doi "https://doi.org/10.1016/0076-6879(95)50066-9" @default.
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