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PMID: 4551144 Published · ppublish English Journal Article

Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin).

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 69 ·No. 2 ·1972-02-00 ·Pages 422-6

Goldberg AL

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.

MeSH Terms
Amino Acids/metabolism Bacterial Proteins/metabolism Biodegradation, Environmental Canavanine/pharmacology Culture Media Cysteine/pharmacology Escherichia coli/drug effects,metabolism Ethylamines/pharmacology Leucine/metabolism Mutation Peptide Chain Initiation, Translational Peptides/metabolism Puromycin/pharmacology Time Factors Tritium
Chemicals
Amino Acids Bacterial Proteins Culture Media Ethylamines Peptides Tritium Canavanine Puromycin Leucine Cysteine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Goldberg A L
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30 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.69.2.422
Published
1972-02-00
Pages
422-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC426471
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.69.2.422 PMC Full Text View journal details
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