Open AccessIdentification of Amino Acid Residues within the N-Terminal Domain of EspA That Play a Role in EspA Filament Biogenesis and Function
Author(s) -
Mona Singh,
Robert K. Shaw,
Stuart Knutton,
Mark J. Pallen,
Valérie F. Crepin,
Gad Frankel
Publication year - 2008
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01753-07
Subject(s) - biogenesis , biology , chaperone (clinical) , escherichia coli , secretion , protein filament , function (biology) , biochemistry , peptide sequence , microbiology and biotechnology , gene , medicine , pathology
EnteropathogenicEscherichia 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.