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Originally published In Press as doi:10.1074/jbc.C000544200 on September 7, 2000

J. Biol. Chem., Vol. 275, Issue 47, 36698-36702, November 24, 2000
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Escherichia coli alpha -Hemolysin (HlyA) Is Heterogeneously Acylated in Vivo with 14-, 15-, and 17-Carbon Fatty Acids*

Kheng B. Limab, Carthene R. Bazemore Walkercd, Lin Guoef, Shahaireen Pellettg, Jeffrey Shabanowitzc, Donald F. Huntch, Erik L. Hewlette, Albrecht Ludwigij, Werner Goebeli, Rodney A. Welchg, and Murray Hackettak

From the a Department of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, the Departments of c Chemistry, e Medicine and Pharmacology, and h Pathology, University of Virginia, Charlottesville, Virginia 22901, the g Department of Medical Microbiology and Immunology, University of Wisconsin, Madison, Wisconsin 53706, and the i Lehrstuhl für Mikrobiologie, Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany

alpha -Hemolysin (HlyA) is a secreted protein virulence factor observed in certain uropathogenic strains of Escherichia coli. The active, mature form of HlyA is produced by posttranslational modification of the protoxin that is mediated by acyl carrier protein and an acyltransferase, HlyC. We have now shown using mass spectrometry that these modifications, when observed in protein isolated in vivo, consist of acylation at the epsilon -amino groups of two internal lysine residues, at positions 564 and 690, with saturated 14- (68%), 15- (26%), and 17- (6%) carbon amide-linked side chains. Thus, HlyA activated in vivo consists of a heterogeneous family of up to nine different covalent structures, and the substrate specificity of the HlyC acyltransferase appears to differ from that of the closely related CyaC acyltransferase expressed by Bordetella pertussis.

* This work was supported by funds from the Department of Medicinal Chemistry and School of Pharmacy, University of Washington, an Amgen postdoctoral fellowship (to M. H.), the David and Lucile Packard Foundation (to C. R. B. W.), National Institutes of Health Grants GM37537 (to D. F. H.), AI18000 (to E. L. H.), and AI20323 (to R. A. W.), and Deutsche Forschungsgemeinschaft Grant SFB 176/B10 (to A. L. and W. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b Present address: Bristol-Myers Squibb Pharmaceutical Research, P. O. Box 4000, Princeton, NJ 08543.

d Present address: Norfolk State University, Norfolk, VA 23504.

f Present address: Immunex Corp., 51 University Street, Seattle, WA 98101.

j Present address: Institute of Medical Microbiology, University of Frankfurt am Main, Paul-Ehrlich-Str. 40, 60596 Frankfurt am Main, Germany.

k To whom correspondence should be addressed: Dept. of Medicinal Chemistry, Box 357610, University of Washington, Seattle, WA 98195. Tel.: 206-616-4586; Fax: 206-685-3252; E-mail: mhackett@u.washington.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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