Thialysine utilization for protein synthesis by an exponentially growing E. coli culture.
The extent of protein lysine substitution by thialysine in E. coli cells grown in media containing the analog depends on the time interval the cells are grown in the presence of analog and on the analog concentration in the medium. By calculating the percent of lysine substitution in newly synthesized proteins it was shown that this reaches, after one cell doubling in the presence of analog, a maximum which is 17% in the cells grown with 0.1 or 0.2 mM thialysine and 8% in cells grown with 0.05 mM thialysine. Proteins synthesized in the presence of analog in the concentration range 0.05-0.2 mM show similar stability to those synthesized in the absence of analog. The extent of analog incorporation into newly synthesized proteins, as regards both the time course and the dependence on analog concentration in the medium, is strictly related to the extent of the repression of AK III, the first enzyme of lysine biosynthetic pathway.
Di Girolamo
M
M
Centro per lo Studio degli Acidi Nucleici del C.N.R., Roma.
Busiello
V
V
Blarzino
C
C
Cini
C
C
D001222:Aspartate Kinase / Q000378:metabolism*; D001426:Bacterial Proteins / Q000032:analysis / Q000096:biosynthesis*; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D004926:Escherichia coli / Q000254:growth & development / Q000378:metabolism*; D008239:Lysine / Q000032:analysis; D010770:Phosphotransferases / Q000378:metabolism*; D013997:Time Factors
D001426:Bacterial Proteins; C000204:S-2-aminoethyl cysteine; D010770:Phosphotransferases; D001222:Aspartate Kinase; D008239:Lysine; D003545:Cysteine