Tetracycline Inhibition of Cell-Free Protein Synthesis I. Binding of Tetracycline to Components of the System

Author:

Day L. E.1

Affiliation:

1. Pfizer Medical Research Laboratories, Chas. Pfizer & Co., Inc., Groton, Connecticut

Abstract

Day , L. E. (Chas. Pfizer & Co., Inc., Groton, Conn.). Tetracycline inhibition of cell-free protein synthesis. I. Binding of tetracycline to components of the system. J. Bacteriol. 91: 1917–1923. 1966.—Tetracycline, an inhibitor of cell-free protein synthesis, effected the dissociation of Escherichia coli 100 S ribosomes to 70 S particles in vivo and in vitro, but was not observed to mediate the further degradation of these particles. The antibiotic was bound by both 50 S (Svedberg) and 30 S subunits of 70 S ribosomes and also by E. coli soluble RNA (sRNA), polyuridylic acid (poly U), and polyadenylic acid (poly A). The binding to ribosomal subunits was higher at 5 × 10 −4 m Mg ++ than at 10 −2 m Mg ++ . The binding to polynucleotide chains was highest when Mg ++ was not added to the reaction mixture.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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