YddG fromEscherichia colipromotes export of aromatic amino acids

Autor: Maria Viacheslavovna Vitushkina, Alexandra Kolokolova, Larisa G. Airich, Vera Georgievna Doroshenko, Vitaliy Arkadyevich Livshits, Sergey V. Mashko
Rok vydání: 2007
Předmět:
Zdroj: FEMS Microbiology Letters. 275:312-318
ISSN: 1574-6968
0378-1097
Popis: 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. colil-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.
Databáze: OpenAIRE