PMID:18178741

Citation	Singh, MP, Shaw, RK, Knutton, S, Pallen, MJ, Crepin, VF and Frankel, G (2008) Identification of amino acid residues within the N-terminal domain of EspA that play a role in EspA filament biogenesis and function. J. Bacteriol. 190:2221-6
Abstract	Enteropathogenic Escherichia coli employs a filamentous type III secretion system, made by homopolymerization of the translocator protein EspA. In this study, we have shown that the N-terminal region of EspA has a role in EspA's protein stability, interaction with the CesAB chaperone, and filament biogenesis and function.
Links	PubMed PMC2258869 Online version:10.1128/JB.01753-07
Keywords	Amino Acids/genetics; Amino Acids/metabolism; Amino Acids/physiology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Fluorescent Antibody Technique; HeLa Cells; Humans; Models, Biological; Mutation; Protein Structure, Tertiary
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.