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J Biol Chem, Vol. 273, Issue 22, 13669-13674, May 29, 1998
From the Institut für Pharmakologie und Toxikologie,
Albert-Ludwigs-Universität Freiburg, Hermann-Herder-Strasse 5, D-79104 Freiburg, Federal Republic of Germany
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.
The Rho-deamidating Cytotoxic Necrotizing Factor 1 from
Escherichia coli Possesses Transglutaminase Activity
CYSTEINE 866 AND HISTIDINE 881 ARE ESSENTIAL FOR ENZYME
ACTIVITY
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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