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Published online before print March 27, 2008, 10.1110/ps.083445408
Protein Science (2008), 17:945-949. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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FOR THE RECORD

The C3 domain of Pasteurella multocida toxin is the minimal domain responsible for activation of Gq-dependent calcium and mitogenic signaling

Leila R. Aminova, Shuhong Luo, Yuka Bannai, Mengfei Ho, and Brenda A. Wilson

Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA

(RECEIVED January 8, 2008; FINAL REVISION February 9, 2008; ACCEPTED February 9, 2008)

The large 1285-amino-acid protein toxin from Pasteurella multocida (PMT) is a multifunctional single-chain polypeptide that binds to and enters eukaryotic cells and acts intracellularly to promote Gq and G12/13 protein-dependent calcium and mitogenic signal transduction. Previous studies indicated that the intracellular activity domain responsible for PMT action was located within the C-terminal 600–700 amino acids. In this study, we have exogenously expressed a series of N- and C-terminal PMT fragments directly in mammalian cells and have used the dual luciferase reporter system to assay for toxin-mediated activation of calcium-calcineurin-NFAT signaling (NFAT-luciferase) and mitogenic serum response signaling (SRE-luciferase). Using this approach, we have defined the last 180 amino acids, which encompass the C3 domain in the crystal structure, as the minimum domain sufficient to activate both NFAT and SRE signaling pathways.

Keywords: dermonecrotic toxin; NFAT; SRE; calcium mobilization; Gq protein


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