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PMID: 5327912 Published · ppublish English Journal Article

Tetracycline inhibition of cell-free protein synthesis. I. Binding of tetracycline to components of the system.

Journal of bacteriology ·Vol. 91 ·No. 5 ·1966-05-00 ·Pages 1917-23

Day LE

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 100S ribosomes to 70S particles in vivo and in vitro, but was not observed to mediate the further degradation of these particles. The antibiotic was bound by both 50S (Svedberg) and 30S subunits of 70S 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 x 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.

MeSH Terms
Adenine Nucleotides Bacterial Proteins/biosynthesis Enzymes Escherichia coli/metabolism In Vitro Techniques Magnesium/pharmacology RNA, Bacterial RNA, Transfer Ribosomes/metabolism Tetracycline/pharmacology Tritium Ultracentrifugation Uracil Nucleotides
Chemicals
Adenine Nucleotides Bacterial Proteins Enzymes RNA, Bacterial Uracil Nucleotides Tritium RNA, Transfer Tetracycline Magnesium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Day L E
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21 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1966-05-00
Pages
1917-23
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC316145
Subset
IM
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