Degradation of thialysine- or selenalysine-containing abnormal proteins in E. coli.
Thialysine and selenalysine can be utilized for protein synthesis by lysine-requiring E. coli cells even in the absence of lysine. Protein synthesis has been determined as labeled leucine incorporation into acid-insoluble material, as increase of cell proteins and as protein-lysine substitution by the analog. Either analog can be incorporated into proteins, in the absence of lysine, for a limited time interval after which cells stop to duplicate. Proteins synthesized during this period contain most of their lysine residues substituted by the analog. Moreover, it has been shown that the analog-containing proteins are unstable and rapidly degraded. Their instability would account for the inability of lysine-requiring E. coli cells to utilize the analog as growth factor.
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000378:metabolism*; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D004926:Escherichia coli / Q000254:growth & development / Q000378:metabolism*; D007930:Leucine / Q000096:biosynthesis; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D016566:Organoselenium Compounds; D012643:Selenium / Q000378:metabolism*
D001426:Bacterial Proteins; D016566:Organoselenium Compounds; C000204:S-2-aminoethyl cysteine; C011351:selenalysine; D007930:Leucine; D012643:Selenium; D008239:Lysine; D003545:Cysteine