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PMID: 5277086 Published · ppublish English Journal Article

A role of aminoacyl-tRNA in the regulation of protein breakdown in Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 68 ·No. 2 ·1971-02-00 ·Pages 362-6

Goldberg AL

Abstract

The rate of degradation of cell proteins in Escherichia coli was studied under various conditions that affect levels of charged tRNA. Protein breakdown increased markedly when the synthesis of valyl-tRNA was prevented in strains containing temperature-sensitive valyl-tRNA synthetase or when the formation of N-formylmethionyl-tRNA was inhibited with trimethoprim. Conversely, protein breakdown decreased in a valine auxotroph-administered valine or an analog capable of attachment to the valyl-tRNA. It appears that changes in the levels of aminoacyl-tRNA regulate protein breakdown by mechanisms similar to those controlling the synthesis of ribosomal RNA. These experiments also demonstrate that protein synthesis is not essential for protein degradation and suggest that the inhibition of degradation in starving cells by chloramphenicol is a secondary effect of the accumulation of charged tRNA.

MeSH Terms
Bacterial Proteins/metabolism Chloramphenicol/pharmacology
Chemicals
Bacterial Proteins Chloramphenicol
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Goldberg A L
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36 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.68.2.362
Published
1971-02-00
Pages
362-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC388938
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.68.2.362 PMC Full Text View journal details
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