Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1

Gudula Schmidt, Peter Sehr, Matthias Wilm, Jörg Selzer, Matthias Mann and Klaus Aktories ()
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Gudula Schmidt: *Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg
Peter Sehr: *Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg
Matthias Wilm: †EMBL
Jörg Selzer: *Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg
Matthias Mann: †EMBL
Klaus Aktories: *Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg

Nature, 1997, vol. 387, issue 6634, 725-729

Abstract: Abstract The actin cytoskeleton is regulated by GTP-hydrolysing proteins, the Rho GTPases1,2, which act as molecular switches in diverse signal-transduction processes3. Various bacterial toxins can inactivate Rho GTPases by ADP-ribosylation1 or glucosylation4. Previous research has identified Rho proteins as putative targets for Escherichia coli cytotoxic necrotizing factors 1 and 2 (CNF1 and 2)5,6. These toxins induce actin assembly and multinucleation in culture cells. Here we show that treatment of RhoA with CNF1 inhibits the intrinsic GTPase activity of RhoA and completely blocks GTPase activity stimulated by the Rho-GTPase-activating protein (rhoGAP). Analysis by mass spectrometry and amino-acid sequencing of proteolytic peptides derived from CNF1-treated RhoA indicate that CNF1 induces deamidation of a glutamine residue at position 63 (Gln 63) to give constitutively active Rho protein.

Date: 1997
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DOI: 10.1038/42735

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