Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin.
Exoenzyme S, which had been thought to be unselective, catalyzes the ADP-ribosylation of only a subset of cellular proteins. The intermediate filament protein vimentin is one of the more abundant substrates. Disassembled vimentin, and proteolytic fragments of vimentin that cannot form filaments, is more readily ADP-ribosylated than is filamentous vimentin.
Coburn
J
J
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
Dillon
S T
ST
Iglewski
B H
BH
Gill
D M
DM
D036002:ADP Ribose Transferases; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D001427:Bacterial Toxins; D015153:Blotting, Western; D003599:Cytoskeleton / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D007382:Intermediate Filaments / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013379:Substrate Specificity; D014746:Vimentin / Q000378:metabolism*
D001427:Bacterial Toxins; D014746:Vimentin; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases; C444820:exoenzyme S