Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin. Infect Immun 1989 Mar;57(3):996-8
Date
03/01/1989Pubmed ID
2492977Pubmed Central ID
PMC313212DOI
10.1128/iai.57.3.996-998.1989Scopus ID
2-s2.0-0024510722 (requires institutional sign-in at Scopus site) 77 CitationsAbstract
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.
Author List
Coburn J, Dillon ST, Iglewski BH, Gill DMAuthor
Jenifer Coburn PhD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ADP Ribose TransferasesAdenosine Diphosphate Ribose
Bacterial Toxins
Blotting, Western
Cytoskeleton
Electrophoresis, Gel, Two-Dimensional
Intermediate Filaments
Poly(ADP-ribose) Polymerases
Pseudomonas aeruginosa
Substrate Specificity
Vimentin