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PMID: 2492977 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin.

Infection and immunity ·Vol. 57 ·No. 3 ·1989-03-00 ·Pages 996-8

Coburn J, Dillon ST, Iglewski BH, Gill DM

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.

MeSH Terms

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

Chemicals

Bacterial Toxins Vimentin Adenosine Diphosphate Ribose ADP Ribose Transferases Poly(ADP-ribose) Polymerases exoenzyme S

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Coburn J

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.

Dillon S T

Iglewski B H

Gill D M

References (17)

17 references, click to expand

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Article Info

Journal

Infection and immunity

Abbr.

Infect Immun

ISSN

0019-9567

DOI

10.1128/iai.57.3.996-998.1989

Published

1989-03-00

Pages

996-8

Language

English

Region

United States

NLM ID

0246127

PMCID

PMC313212

Subset

Grants

NIAID NIH HHS · AI 16928 · United States

NIAID NIH HHS · AI 25669 · United States

External Links

PubMed source DOI: 10.1128/iai.57.3.996-998.1989 PMC Full Text View journal details

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Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin.

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