Degradation of Abnormal Proteins in Escherichia coli
- 1 February 1972
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 69 (2) , 422-426
- https://doi.org/10.1073/pnas.69.2.422
Abstract
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.Keywords
This publication has 24 references indexed in Scilit:
- INFORMATIONAL SUPPRESSIONAnnual Review of Genetics, 1970
- In vivo Degradation of Nonsense Fragments in E. coliNature, 1970
- In vivo Degradation of Mutant Lac RepressorNature, 1970
- A ribosomal ambiguity mutationJournal of Molecular Biology, 1969
- Mechanism of canavanine death in Escherichia coliJournal of Molecular Biology, 1968
- Turnover of protein in Escherichia coli starving for nitrogenBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1966
- Characteristics of the inhibition of hemoglobin synthesis in rabbit reticulocytes by threo-α-amino-β-chlorobutyric acidBiochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects, 1964
- PUROMYCIN INHIBITION OF PROTEIN SYNTHESIS: INCORPORATION OF PUROMYCIN INTO PEPTIDE CHAINSProceedings of the National Academy of Sciences, 1964
- Der N-Stoffwechsel bei der Erythrocytenreifung: Die N-Bilanz unter endogenen BedingungenHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1958
- STRUCTURE AND ENZYMATIC BREAK-DOWN OF PROTEINSPublished by Cold Spring Harbor Laboratory ,1950