Abstract
Day , L. E. (Chas. Pfizer & Co., Inc., Groton, Conn.). Tetracycline inhibition of cell-free protein synthesis. II. Effect of the binding of tetracycline to the components of the system. J. Bacteriol. 92: 197–203. 1966.—When tetracycline, an inhibitor of cell-free protein synthesis, was preincubated with each component of the Escherichia coli cell-free system, i.e., ribosomes, soluble ribonucleic acid (sRNA), polyuridylic acid (poly U), and S-100 (supernatant enzymes), only the ribosomal-bound antibiotic was inhibitory to the cell-free assay. Experiments designed to further localize the site of inhibition to either the 50 S (Svedberg) or the 30 S ribosomal subunit were not conclusive. Tritiated tetracycline (7-H 3 -tetracycline) was bound to isolated 50 S ribosomes, and these were recombined with 30 S subunits to form 70 S ribosomes. When these ribosomes were dissociated and the subunits reisolated, the antibiotic was found with both the 50 S and the 30 S particles. The same results were observed when the tetracycline was initially bound to the 30 S subunit.
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Dates
Type | When |
---|---|
Created | 5 years, 7 months ago (Jan. 4, 2020, 8:54 p.m.) |
Deposited | 4 years, 1 month ago (July 29, 2021, 1:21 p.m.) |
Indexed | 11 months, 3 weeks ago (Sept. 6, 2024, 10:24 a.m.) |
Issued | 59 years, 2 months ago (July 1, 1966) |
Published | 59 years, 2 months ago (July 1, 1966) |
Published Print | 59 years, 2 months ago (July 1, 1966) |
@article{Day_1966, title={Tetracycline Inhibition of Cell-Free Protein Synthesis II. Effect of the Binding of Tetracycline to the Components of the System}, volume={92}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.92.1.197-203.1966}, DOI={10.1128/jb.92.1.197-203.1966}, number={1}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Day, L. E.}, year={1966}, month=jul, pages={197–203} }