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. 1972 Feb;69(2):422–426. doi: 10.1073/pnas.69.2.422

Degradation of Abnormal Proteins in Escherichia coli

Alfred L Goldberg 1
PMCID: PMC426471  PMID: 4551144

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: protein breakdown, protein structure, mistranslation, amino acid analogs, puromycin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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