Publications
1993
Roth A, Eriani G, Dirheimer G, Gangloff J
Kinetic properties of pure overproduced Bacillus subtilis phenylalanyl-tRNA synthetase do not favour its in vivo inhibition by ochratoxin A Journal Article
In: FEBS Lett, vol. 326, no. 1-3, pp. 87-91, 1993, ISBN: 8325392, (0014-5793 Journal Article).
Abstract | Links | BibTeX | Tags: Bacillus subtilis/drug effects/*enzymology Binding, Bacterial, Competitive Escherichia coli/enzymology/genetics Kinetics Macromolecular Systems Ochratoxins/*pharmacology Phenylalanine/metabolism Phenylalanine-tRNA Ligase/antagonists & inhibitors/*metabolism Support, ERIANI, Non-U.S. Gov't Transformation, Unité ARN
@article{,
title = {Kinetic properties of pure overproduced Bacillus subtilis phenylalanyl-tRNA synthetase do not favour its in vivo inhibition by ochratoxin A},
author = {A Roth and G Eriani and G Dirheimer and J Gangloff},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8325392},
isbn = {8325392},
year = {1993},
date = {1993-01-01},
journal = {FEBS Lett},
volume = {326},
number = {1-3},
pages = {87-91},
abstract = {Ochratoxine A (OTA) inhibits growth of Bacillus subtilis at pHs below 7. Since OTA is a phenylalanine analogue, this effect could be due to inhibition of phenylalanine-tRNA synthetase (PheRS) by competition of this mycotoxin with the amino acid. Homogeneous PheRS was purified from Bacillus subtilis and from E. coli transformed with the PheRS gene. The latter produced about 40 times more PheRS than B. subtilis. The Km and Ki values of PheRS, respectively, for phenylalanine and OTA were measured and their concentrations within the cell determined. It appears that the concentration of OTA in the cell, in spite of a 25-fold accumulation, remained too low to significantly compete with phenylalanine. This does not suggest PheRS to be the target of OTA in cell growth and protein synthesis inhibition in Bacillus subtilis. It was also shown that the 2-3-fold increase of PheRS in OTA-treated cells is not due to phenylalanine-controlled attenuation regulation.},
note = {0014-5793
Journal Article},
keywords = {Bacillus subtilis/drug effects/*enzymology Binding, Bacterial, Competitive Escherichia coli/enzymology/genetics Kinetics Macromolecular Systems Ochratoxins/*pharmacology Phenylalanine/metabolism Phenylalanine-tRNA Ligase/antagonists & inhibitors/*metabolism Support, ERIANI, Non-U.S. Gov't Transformation, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Ochratoxine A (OTA) inhibits growth of Bacillus subtilis at pHs below 7. Since OTA is a phenylalanine analogue, this effect could be due to inhibition of phenylalanine-tRNA synthetase (PheRS) by competition of this mycotoxin with the amino acid. Homogeneous PheRS was purified from Bacillus subtilis and from E. coli transformed with the PheRS gene. The latter produced about 40 times more PheRS than B. subtilis. The Km and Ki values of PheRS, respectively, for phenylalanine and OTA were measured and their concentrations within the cell determined. It appears that the concentration of OTA in the cell, in spite of a 25-fold accumulation, remained too low to significantly compete with phenylalanine. This does not suggest PheRS to be the target of OTA in cell growth and protein synthesis inhibition in Bacillus subtilis. It was also shown that the 2-3-fold increase of PheRS in OTA-treated cells is not due to phenylalanine-controlled attenuation regulation.