Aspartokinase III repression in a thialysine-resistant mutant of E. coli.
A thialysine-resistant mutant of the E. coli KL16 strain was isolated. It can grow equally well in the presence and in the absence of thialysine. The properties of the two lysine transport systems, of the lysyl-tRNA synthetase and of the aspartokinase III (AK III) were studied in the mutant and in the parent strain. AK III is the first enzyme of the lysine biosynthetic pathway and its activity is involved in the regulation of lysine biosynthesis by feed-back and repression mechanism. No difference between the two strains was evidenced as regards 1) the affinity of the transport systems for lysine and thialysine 2) the activity of the lysyl-tRNA synthetase 3) the allosteric inhibition of the AK III by lysine and thialysine. A marked difference between the two strains has been evidenced in the AK III repression: in the mutant the enzyme is much less repressed both by lysine and thialysine. The possible correlation between the activity of AK III and the thialysine-resistance is discussed in this paper.
Di Girolamo
M
M
Dipartimento di Scienze e Tecnologie, Biomediche e di Biometria-Università dell'Aquila.
Busiello
V
V
Di Girolamo
A
A
Foppoli
C
C
De Marco
C
C
D001222:Aspartate Kinase / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D001693:Biological Transport, Active; D003545:Cysteine / Q000031:analogs & derivatives* / Q000494:pharmacology; D004352:Drug Resistance, Microbial / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D007700:Kinetics; D008239:Lysine / Q000378:metabolism / Q000494:pharmacology; D008250:Lysine-tRNA Ligase / Q000378:metabolism; D009154:Mutation; D010770:Phosphotransferases / Q000378:metabolism*
C000204:S-2-aminoethyl cysteine; D010770:Phosphotransferases; D001222:Aspartate Kinase; D008250:Lysine-tRNA Ligase; D008239:Lysine; D003545:Cysteine