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The Rho-deamidating cytotoxic necrotizing factor 1 from Escherichia coli possesses transglutaminase activity. Cysteine 866 and histidine 881 are essential for enzyme activity
Albert-Ludwigs-Universität Freiburg, Germany.
Albert-Ludwigs-Universität Freiburg, Germany.
Albert-Ludwigs-Universität Freiburg, Germany.
Albert-Ludwigs-Universität Freiburg, Germany.
1998 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 273, no 22, 13669-13674 p.Article in journal (Refereed) Published
Abstract [en]

Recently, it has been reported that cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli induces formation of stress fibers by deamidation of glutamine 63 of RhoA (Schmidt, G., Sehr, P., Wilm, M., Selzer, J., Mann, M., and Aktories, K. (1997) Nature 387, 725-729); Flatau, G., Lemichez, E., Gauthier, M., Chardin, P., Paris, S., Fiorentini, C., and Boquet, P. (1997) Nature 387, 729-733). By using mass spectrometric analysis, we show now that the toxin transfers ethylenediamine, putrescine, and dansylcadaverine specifically onto glutamine 63 of RhoA. RhoA was also a substrate for guinea pig liver transglutaminase, which modified not only glutamine 63, but also glutamine residues at positions 52 and 136. Treatment of the fully active N-terminal fragment of CNF1 (amino acid residues 709-1014) with iodoacetamide inhibited both deamidation and transglutamination activities. Moreover, exchange of cysteine 866 with serine blocked the enzyme activity of the N-terminal CNF1 fragment. In addition, we identified histidine 881 to be essential for the enzyme activity of CNF1. The data indicate that CNF1 shares a catalytic dyad of cysteine and histidine residues with eukaryotic transglutaminases and cysteine proteases.

Place, publisher, year, edition, pages
American Society for Biochemistry and Molecular Biology, 1998. Vol. 273, no 22, 13669-13674 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-99617DOI: 10.1074/jbc.273.22.13669PubMedID: 9593707OAI: oai:DiVA.org:liu-99617DiVA: diva2:657389
Available from: 2013-10-18 Created: 2013-10-18 Last updated: 2017-12-06Bibliographically approved

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Lerm, Maria

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