Cell-free fatty acid acylation of Semliki Forest viral polypeptides with microsomal membranes from eukaryotic cells.

Newly synthesized G protein of vesicular stomatitis virus is not transported to the Golgi complex in mitotic cells.

“…If this interpretation is correct, the absence of endo H-sensitive, fatty acylated G protein in mitotic cells suggests that the rough ER and transitional elements are functionally, and possibly also physically, separated during mitosis. In this instance we cannot draw any conclusions about inhibition of vesicular transport between the ER and Golgi complex, and will only be able to do so when the fatty acylation enzyme can be located by subeellular fractionation using a direct assay such as that described by Berger and Schmidt (1984).…”

The covalent modification of eukaryotic proteins with lipid.

“…The palmityl transferase may be a cytoplasmic protein because palmitic acid is usually found in regions of proteins interacting with the cytoplasmic face of membranes. The donor is likely to be palmityl CoA (3).…”

Possible Roles of Long-chain Fatty Acyl-CoA Esters in the Fusion of Biomembranes

“…Palmitoylation of proteins refers to the posttranslational modification in which palmitic acid is covalently attached to cysteine residues via a thioester bond (Towler et al, 1988;Schultz et al, 1988). Despite the early identification of LCACoA esters as the immediate donor of acyl-groups (Bizzozero and Lees, 1986;Berger and Schmidt, 1984a) and the development of a number of cell-free acylation systems (Gutierrez and Magee, 1991;Mack et al, 1987;Berger and Schmidt, 1984b), there have only been a few protein-acyl transferases described. A number of proteins can be acylated in a cell-free system via a non-enzymatic transacylation reaction between LCACoA esters and thiol-groups on the proteins.…”

“…A number of proteins can be acylated in a cell-free system via a non-enzymatic transacylation reaction between LCACoA esters and thiol-groups on the proteins. These include, for example, rhodopsin (Moench et al, 1994;Oibrien et al, 1987), myelin PO glycoprotein (Bharadwaj and Bizzozero, 1995), myelin proteolipid protein (Ross and Braun, 1988;Bizzozero et al, 1987a), Semliki Forest virus E2 glycoprotein (Berger and Schmidt, 1984b), the α-subunit of certain heterotrimeric G-proteins (Duncan and Gilman, 1996), pulmonary surfactant protein SP-C (Qanbar and Possmayer, 1994) as well as some synthetic cysteine-containing peptides (Bharadwaj and Bizzozero, 1995;Quesnel and Silvius, 1994). The biological significance of autoacylation of proteins is unknown, but it is interesting that the palmitoylated cysteine residues in myelin proteolipid protein modified in vivo are also autoacylated in vitro and that addition of cell extracts to cell-free autoacylation assays in some cases do not enhance protein acylation (Bizzozero et al, 1987b;Bizzozero and Lees, 1986).…”