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Science 21 October 1994:
Vol. 266. no. 5184, pp. 433 - 435
DOI: 10.1126/science.7939682
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Articles

Science, Vol 266, Issue 5184, 433-435
Copyright © 1994 by American Association for the Advancement of Science

articles

Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis

M Hackett, L Guo, J Shabanowitz, DF Hunt, and EL Hewlett

Department of Chemistry, University of Virginia, Charlottesville 22901.

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.


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