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PMID: 11895993 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Membrane localization contributes to the in vivo ADP-ribosylation of Ras by Pseudomonas aeruginosa ExoS.

Infection and immunity ·Vol. 70 ·No. 4 ·2002-04-00 ·Pages 2230-2

Riese MJ, Barbieri JT

Abstract

Type III-delivered exoenzyme S (ExoS) preferentially ADP-ribosylated membrane-associated His(6)HRas, relative to its cytosolic derivative His(6)HRas Delta CAAX. This indicates that the subcellular protein distribution contributes to in vivo ADP-ribosylation by ExoS.

MeSH Terms
ADP Ribose Transferases/metabolism Adenosine Diphosphate Ribose/metabolism Animals Bacterial Toxins CHO Cells Cell Membrane/metabolism Cricetinae Pseudomonas aeruginosa/enzymology ras Proteins/metabolism
Chemicals
Bacterial Toxins Adenosine Diphosphate Ribose ADP Ribose Transferases exoenzyme S ras Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Riese Matthew J
Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA.
Barbieri Joseph T
References (13)
13 references, click to expand
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
2002-04-00
Pages
2230-2
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC127869
Subset
IM
Grants
NIAID NIH HHS · AI-31062 · United States
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