Identification of amino acid residues within the N-terminal domain of EspA that play a role in EspA filament biogenesis and function.
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.
Singh
Mona P
MP
Division of Cell and Molecular Biology, Imperial College, London SW7 2AZ, United Kingdom.
Shaw
Robert K
RK
Knutton
Stuart
S
Pallen
Mark J
MJ
Crepin
Valerie F
VF
Frankel
Gad
G
D000596:Amino Acids / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D008954:Models, Biological; D009154:Mutation; D017434:Protein Structure, Tertiary
D000596:Amino Acids; D029968:Escherichia coli Proteins; C102051:EspA protein, E coli