Hackett M, Guo L, Shabanowitz J, Hunt D F, Hewlett E L
Department of Chemistry, University of Virginia, Charlottesville 22901.
Science. 1994 Oct 21;266(5184):433-5. doi: 10.1126/science.7939682.
A number of bacterial protein toxins, including adenylate cyclase (AC) toxin from Bordetella pertussis, require the product of an accessory gene in order to express their biological activities. In this study, mass spectrometry was used to demonstrate that activated, wild-type AC toxin was modified by amide-linked palmitoylation on the epsilon-amino group of lysine 983. This modification was absent from a mutant in which the accessory gene had been disrupted. A synthetic palmitoylated peptide corresponding to the tryptic fragment (glutamine 972 to arginine 984) that contained the acylation blocked AC toxin-induced accumulation of adenosine 3',5'-monophosphate, whereas the non-acylated peptide had no effect.
许多细菌蛋白毒素，包括百日咳博德特氏菌的腺苷酸环化酶（AC）毒素，需要一个辅助基因的产物来表达其生物学活性。在本研究中，使用质谱法证明活化的野生型AC毒素在赖氨酸983的ε-氨基上通过酰胺连接的棕榈酰化进行了修饰。在辅助基因被破坏的突变体中不存在这种修饰。与包含酰化位点的胰蛋白酶片段（谷氨酰胺972至精氨酸984）相对应的合成棕榈酰化肽可阻断AC毒素诱导的3',5'-单磷酸腺苷的积累，而非酰化肽则没有效果。
