F. Hofmann et al., THE RAS-RELATED PROTEIN RAL IS MONOGLUCOSYLATED BY CLOSTRIDIUM-SORDELLII LETHAL TOXIN, Biochemical and biophysical research communications, 227(1), 1996, pp. 77-81
Clostridium sordellii lethal toxin (LT), a cytotoxin which causes pref
erential destruction of the actin cytoskeleton, has been recently iden
tified as glucosyltransferase to modify the low molecular mass GTPases
Rac, Ras and Rap. We report here on LT produced by C. sordellii strai
n 6018 which glucosylates in addition lo Rac, Ras and Rap the Ral prot
ein. LT from strain VPI9048 however does not glucosylate Ral. Besides
recombinant Ral, cellular Ral is also substrate. In the GDP-bound form
, Ral is a superior substrate to the GTP form. Acceptor amino acid for
glucose is threonine-46 which is equivalent to threonine-35 in H-Ras
located in the effector region. The Ral-glucosylating toxin is a novel
isoform of Ras-modifying clostridial cytotoxins. (C) 1996 Academic Pr
ess, Inc.