Directed in vivo post translational modification in a different host

Post-translational modifications are an essential part of protein function. One modification that is particularly difficult to study is farnesylation. This modification adds a large hydrophobic chain to the protein, allowing it to interact with lipid membranes. It also unfortunately significantly lowers the solubility of the protein it is attached to. Studying this modification is particularly difficult in its native environment as they are generally associated with strongly binding cofactors (usually to counteract the effects of the hydrophobic modification). Here we show a method to not only express and farnesylate a protein in a non-native background, but we also discuss the methods for its purifications and characterization.