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PMID: 8468279 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement.

Journal of bacteriology ·Vol. 175 ·No. 8 ·1993-04-00 ·Pages 2189-96

Goldberg MB, Bârzu O, Parsot C, Sansonetti PJ

Abstract

Shigella flexneri uses elements of the host cell cytoskeleton to move within cells and from cell to cell. IcsA, an S. flexneri protein involved in this movement, was purified and studied in vitro. IcsA bound the radiolabelled ATP analog 3'(2')-O-(4-benzoyl)benzoyl-ATP and hydrolyzed ATP. In addition, the surface localization of IcsA on both extracellular and intracellular shigellae was unipolar. Further, in HeLa cells infected with shigellae, IcsA antiserum labelled the actin tail throughout its length, thereby suggesting that IcsA interacts with elements within the tail. Localization of IcsA within the tail at a distance from the bacterium would require its secretion; we demonstrate here that in vitro IcsA is secreted into the culture supernatant in a cleaved form.

MeSH Terms
Adenosine Triphosphatases/analysis Adenosine Triphosphate/metabolism Amino Acid Sequence Bacterial Proteins/analysis,chemistry,isolation & purification,metabolism Cell Movement DNA-Binding Proteins Escherichia coli/metabolism HeLa Cells Humans Molecular Sequence Data Shigella flexneri/chemistry Transcription Factors
Chemicals
Bacterial Proteins DNA-Binding Proteins Transcription Factors virG protein, Shigella flexneri Adenosine Triphosphate Adenosine Triphosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Goldberg M B
Unité de Pathogénie Microbienne Moléculaire, Institut Pasteur, Paris, France.
Bârzu O
Parsot C
Sansonetti P J
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1993-04-00
Pages
2189-96
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC204503
Subset
IM
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