Open AccessRole of the carboxy‐terminal region of the outer membrane protein AatA in the export of dispersin from enteroaggregative Escherichia coli
Author(s) -
Iwashita Mayumi,
Nishi Junichiro,
Wakimoto Naoko,
Fujiyama Rika,
Yamamoto Kimie,
Tokuda Koichi,
Manago Kunihiro,
Kawano Yoshifumi
Publication year - 2006
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00123.x
Subject(s) - bacterial outer membrane , escherichia coli , mutant , mutagenesis , amino acid , site directed mutagenesis , enteroaggregative escherichia coli , biology , biochemistry , chemistry , microbiology and biotechnology , enterobacteriaceae , gene
Enteroaggregative Escherichia coli (EAEC) is an emerging enteric pathogen in both developing and industrialized countries. AatA, an outer‐membrane protein that is a homolog of E. coli TolC, facilitates the export of the dispersin protein Aap across the outer membrane in EAEC. To identify which amino acids are important for this export activity, site‐directed mutagenesis of the carboxy terminus was performed. An insertional mutant of aatA was complemented with each of several deletion mutants, and was examined for Aap secretion. The results showed that three nonpolar amino acids at positions 381–383 (Phe–Leu–Leu) were required for the activity, and these residues were located at the base of carboxy‐terminal elongation in the equatorial domain of AatA.