The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition.

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Abstract
The transmembrane glycoprotein (G protein) of vesicular stomatitis virus (VSV) is known to contain 1-2 mol of covalently linked fatty acid (pamitate)/mol of protein. G protein is oriented in cellular membranes such that the carboxyl-terminal 29 amino acids protrude into the cytoplasm. Expression in eukaryotic [African green monkey kidney]cells of mutagenized c[complementary]DNA clones that encode VSV G proteins lacking portions of this cytoplasmic domain was obtained. Labeling of these truncated proteins with [3H]palmitate indicated that the palmitate might be linked to an amino acid residue within the first 14 residues on the carboxyl-terminal side of the transmembrane domain. Using oligonucleotide directed mutagenesis, the single codon specifying cysteine in this domain was changed to a codon specifying serine. Expression of this mutant gene results in synthesis of a G protein lacking palmitate. Evidently, linkage of palmitate to G protein is through the cysteine in the cytoplasmic domain, and such a linkage may occur in many viral and cellular glycoproteins. The G protein lacking palmitate is glycosylated and is transported normally to the cell surface.