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 |
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Rok vydání: | 2007 |
Předmět: |
Phenylalanine
Biology medicine.disease_cause Microbiology Amino Acids Aromatic chemistry.chemical_compound Escherichia coli Genetics medicine Aromatic amino acids Inner membrane Tyrosine Molecular Biology Gene chemistry.chemical_classification Escherichia coli Proteins Tryptophan Membrane Proteins Gene Expression Regulation Bacterial Molecular biology Culture Media Amino acid Protein Transport Biochemistry chemistry |
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 |
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