CsrA and TnaB coregulate tryptophanase activity to promote exotoxin-induced killing of Caenorhabditis elegans by enteropathogenic Escherichia coli.

Abstract

Enteropathogenic Escherichia coli(EPEC) requires the tnaA-encoded enzyme tryptophanase and its substrate tryptophan to synthesize diffusible exotoxins that kill the nematode Caenorhabditis elegans. Here, we demonstrate that the RNA-binding protein CsrA and the tryptophan permease TnaB coregulate tryptophanase activity, through mutually exclusive pathways, to stimulate toxin-mediated paralysis and killing of C. elegans.

• Authors: Shantanu Bhatt, Akwasi Anyanful, Daniel Kalman
• Journal: Journal of bacteriology (J Bacteriol) Vol. 193 Issue 17 Pg. 4516-22 (Sep 2011) ISSN: 1098-5530 [Electronic] United States
• PMID: 21705596 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, U.S. Gov't, Non-P.H.S.)

Chemical References

• Amino Acid Transport Systems
• CsrA protein, E coli
• Escherichia coli Proteins
• Exotoxins
• RNA-Binding Proteins
• Repressor Proteins
• TnaB protein, E coli
• Tryptophan
• Tryptophanase

Topics

• Amino Acid Sequence
• Amino Acid Transport Systems (genetics, metabolism)
• Animals
• Base Sequence
• Caenorhabditis elegans (microbiology)
• Enteropathogenic Escherichia coli (enzymology, genetics, pathogenicity)
• Escherichia coli Proteins (genetics, metabolism)
• Exotoxins (metabolism)
• Gene Expression Regulation, Bacterial
• Molecular Sequence Data
• Operon
• RNA-Binding Proteins (genetics, metabolism)
• Repressor Proteins (genetics, metabolism)
• Tryptophan (metabolism)
• Tryptophanase (genetics, metabolism)