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

Abstract:

:The actin cytoskeleton is regulated by GTP-hydrolysing proteins, the Rho GTPases, which act as molecular switches in diverse signal-transduction processes. Various bacterial toxins can inactivate Rho GTPases by ADP-ribosylation or glucosylation. Previous research has identified Rho proteins as putative targets for Escherichia coli cytotoxic necrotizing factors 1 and 2 (CNF1 and 2). 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.

journal_name

Nature

journal_title

Nature

authors

Schmidt G,Sehr P,Wilm M,Selzer J,Mann M,Aktories K

doi

10.1038/42735

subject

Has Abstract

pub_date

1997-06-12 00:00:00

pages

725-9

issue

6634

eissn

0028-0836

issn

1476-4687

journal_volume

387

pub_type

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