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• W1991498982 abstract "Recently, it has been reported that cytotoxic necrotizing factor 1 (CNF1) from <i>Escherichia coli</i>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) <i>Nature</i> 387, 725–729); Flatau, G., Lemichez, E., Gauthier, M., Chardin, P., Paris, S., Fiorentini, C., and Boquet, P. (1997) <i>Nature</i> 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." @default.
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• W1991498982 date "1998-05-01" @default.
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• W1991498982 title "The Rho-deamidating Cytotoxic Necrotizing Factor 1 fromEscherichia coli Possesses Transglutaminase Activity" @default.
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• W1991498982 doi "https://doi.org/10.1074/jbc.273.22.13669" @default.
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