Faculty Collaboration Database

Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin. Infect Immun 1989 Mar;57(3):996-8 PMID: 2492977 PMCID: PMC313212

Pubmed ID

2492977

Abstract

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 DM

Author

Jenifer Coburn PhD Professor in the Medicine department at Medical College of Wisconsin

Scopus

2-s2.0-0024510722   66 Citations

MESH terms used to index this publication - Major topics in bold

ADP Ribose Transferases
Adenosine Diphosphate Ribose
Bacterial Toxins
Blotting, Western
Cytoskeleton
Electrophoresis, Gel, Two-Dimensional
Intermediate Filaments
Poly(ADP-ribose) Polymerases
Pseudomonas aeruginosa
Substrate Specificity
Vimentin