Aspartokinase III repression and lysine analogs utilization for protein synthesis.
The extents of thialysine and selenalysine incorporation into cell proteins were compared in E. coli KL16 and in a mutant able to grow equally well in the presence or in the absence of both lysine analogs. The mutant differs from the parental strain in the repression of aspartokinase III (AKIII), the first enzyme of the lysine biosynthetic pathway. No analog incorporation into proteins was observed in mutant cells grown in the presence of either analog, whereas a marked analog incorporation was observed in the parental strain, where up to 17% and 12% of protein lysine can be substituted by thialysine and selenalysine respectively. In the parental strain grown in media containing either analog at different concentration the extent of analog incorporation into proteins is related to the extent of AKIII repression.
Di Girolamo
M
M
Dipartimento di Scienze e Tecnologie Biomediche e Biometria, Università dell'Aquila, Italy.
Busiello
V
V
Coccia
R
R
Foppoli
C
C
D001222:Aspartate Kinase / Q000096:biosynthesis* / Q000235:genetics; D003545:Cysteine / Q000031:analogs & derivatives / Q000378:metabolism; D004794:Enzyme Repression; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D007527:Isoenzymes; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism*; D009154:Mutation; D016566:Organoselenium Compounds; D014176:Protein Biosynthesis; D012643:Selenium / Q000378:metabolism
D007527:Isoenzymes; D016566:Organoselenium Compounds; C000204:S-2-aminoethyl cysteine; C011351:selenalysine; D001222:Aspartate Kinase; D012643:Selenium; D008239:Lysine; D003545:Cysteine