Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin).
Evidence is presented that E. coli contains a mechanism for selective degradation of abnormal proteins. Unfinished polypeptides containing puromycin, proteins containing frequent errors in translation, such as those synthesized by strains containing a ram mutation or a missense suppressor, and proteins containing amino-acid analogs were degraded more rapidly than were normal cell proteins. The degradation of analog- or puromycin-containing proteins appears to be an energy-dependent process. Unlike normal proteins, such proteins were degraded at similar rates by growing and by nongrowing cells.
D000596:Amino Acids / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001673:Biodegradation, Environmental; D002172:Canavanine / Q000494:pharmacology; D003470:Culture Media; D003545:Cysteine / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D005021:Ethylamines / Q000494:pharmacology; D007930:Leucine / Q000378:metabolism; D009154:Mutation; D010442:Peptide Chain Initiation, Translational; D010455:Peptides / Q000378:metabolism; D011691:Puromycin / Q000494:pharmacology; D013997:Time Factors; D014316:Tritium
D000596:Amino Acids; D001426:Bacterial Proteins; D003470:Culture Media; D005021:Ethylamines; D010455:Peptides; D014316:Tritium; D002172:Canavanine; D011691:Puromycin; D007930:Leucine; D003545:Cysteine