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 hydrophobic residues is often found near the palmitoylated cysteine, the role of these residues in the selection of specific palmitoylation sites was assessed. Short peptides derived from the beta(2)-adrenergic receptor sequence, modified to present different proportions of basic, acidic and hydrophobic residues, 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 short peptides contain the required molecular determinants leading to selective S-acylation. Whether or not these sequence characteristics also contribute to the selectivity of palmitoylation in vivo will need to be further investigated.
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Département de Biochimie and Groupe de Recherche sur le Système Nerveux Autonome, Université de Montréal, C.P. 6128, succursale Centre-Ville, H3C 3J7, Montréal, QC, Canada.
Ansanay
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Qanbar
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Bouvier
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D000215:Acylation; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D019308:Palmitic Acid / Q000378:metabolism*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D018343:Receptors, Adrenergic, beta-2 / Q000737:chemistry* / Q000378:metabolism*
D000596:Amino Acids; D010446:Peptide Fragments; D018343:Receptors, Adrenergic, beta-2; D019308:Palmitic Acid; D003545:Cysteine