Open AccessYddG from Escherichia coli promotes export of aromatic amino acids
Author(s) -
Doroshenko Vera,
Airich Larisa,
Vitushkina Maria,
Kolokolova Alexandra,
Livshits Vitaliy,
Mashko Sergey
Publication year - 2007
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.1574-6968.2007.00894.x
Subject(s) - phenylalanine , aromatic amino acids , escherichia coli , tryptophan , tyrosine , amino acid , biochemistry , strain (injury) , chemistry , biology , gene , anatomy
The inner membrane protein YddG of Escherichia coli is a homologue of the known amino acid exporters RhtA and YdeD. It was found that the yddG gene overexpression conferred resistance upon E. coli cells to the inhibiting concentrations of l ‐phenylalanine and aromatic amino acid analogues, dl ‐ p ‐fluorophenylalanine, dl ‐ o ‐fluorophenylalanine and dl ‐5‐fluorotryptophan. In addition, yddG overexpression enhanced the production of l ‐phenylalanine, l ‐tyrosine or l ‐tryptophan by the respective E. coli ‐producing strains. On the other hand, the inactivation of yddG decreased the aromatic amino acid accumulation by these strains. The cells of the E. coli l ‐phenylalanine‐producing strain containing overexpressed yddG accumulated less l ‐phenylalanine inside and exported the amino acid at a higher rate than the cells of the isogenic strain containing wild‐type yddG . Taken together, these results indicate that YddG functions as an aromatic amino acid exporter.