Acylation of viral and eukaryotic proteins.

Post-translational modification has long been recognized as a way in which the properties of protein molecules may be subtly altered after synthesis of the polypeptide chain is complete. Amongst the moieties most commonly encountered covalently attached to proteins are acetyl and formyl groups, phosphate groups and carbohydrates. These modifications have been a source of study for many years, but in the last decade it has become apparent that the binding of lipids to proteins is also widespread and certainly of great importance to the correct functioning of the organism. The first protein reported to contain covalently attached fatty acid was purified on the basis of its solubility in organic solvents and has been termed myelin proteolipid (Folch & Lees, 1951). It was considered for some time that this phenomenon was restricted to the unusual circumstances pertaining to the myelin sheath. However, over the past decade it has become apparent that this is not the case and acyl proteins are widespread both in eukaryotic cell membranes and in viruses. It is my intention to review here the current state of our knowledge of these systems. This seems a particularly appropriate time as the area of research has taken on an exciting new aspect with the realization that acylation is