Primary sequence requirements for S-acylation of beta(2)-adrenergic receptor peptides

Palmitoylation is a post-translational modification that occurs on selected cysteines of many proteins. Since a high proportion of basic and hydrophob ic residues is often found near the palmitoylated cysteine, the role of the se residues in the selection of specific palmitoylation sites was assessed. Short peptides derived from the beta (2)-adrenergic receptor sequence, mod ified to present different proportions of basic, acidic and hydrophobic res idues, were tested in an in vitro S-acylation assay. Basic residues proved to be essential, whereas hydrophobic residues greatly enhanced S-acylation and acidic residues inhibited it. Taken together, these results show that s hort peptides contain tile required molecular determinants leading to selec tive S-acylation. Whether or not these sequence characteristics also contri bute to the selectivity of palmitoylation in vivo will need to be further i nvestigated. (C) 2001 Published by Elsevier Science B.V. on behalf of the F ederation of European Biochemical Societies.