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[Oxytetracycline binding to E. coli ribosomes]. 1975

S A Strel'tsov, and M K Kukhanova, and G V Gurskiĭ, and A A Kraevskiĭ, and I V Beliavskaia

Binding of oxytetracycline to E. coli ribosomes was studied by equilibrium dialysis. The results are consistent with the existence of two classes of binding sites for the antibiotic on ribosomes having different reactivities. There is one strong binding site as well as about 500 weak ones. The association constant for strong complexes is about 10(3) times greater than the value for weak ones. Oxytetracycline and tetracycline bind to ribosomes as magnesium chelates. Increase of the concentration of Mg2+ leads to the formation of two types of magnesium chelates of the antibiotic: chelate 1 which is formed at a relatively low concentration of Mg2+ and has a stiochiometry 1:1, and chelate 2 which probably corresponds to the attachment of second ion to the antibiotic molecule. The strong binding of oxytetracycline to ribosomes prevents the template dependent association of aminoacyl-tRNA with ribosomes. However, no changes in the extent of the antibiotic binding were found upon addition of aminoacyl-tRNA, poly(U) and chloramphenicol to oxytetracycline-ribosome complexes. It has been suggested that inhibiting effect of oxytetracycline on the protein synthesis involves an allosteric mechanism.

UI MeSH Term Description Entries
D008274 Magnesium A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
D010118 Oxytetracycline A TETRACYCLINE analog isolated from the actinomycete STREPTOMYCES RIMOSUS and used in a wide variety of clinical conditions. Hydroxytetracycline,Bisolvomycin,Geomycin,Oxyterracin,Oxyterracine,Oxytetracid,Oxytetracycline Anhydrous,Oxytetracycline Calcium,Oxytetracycline Dihydrate,Oxytetracycline Hydrochloride,Oxytetracycline Monohydrochloride,Oxytetracycline Sulfate (2:1),Oxytetracycline, (4a beta,5 beta,5a beta,12a beta)-Isomer,Oxytetracycline, (5 beta)-Isomer,Oxytetracycline, Anhydrous,Oxytetracycline, Calcium (1:1) Salt,Oxytetracycline, Disodium Salt, Dihydrate,Oxytetracycline, Sodium Salt,Terramycin
D011072 Poly U A group of uridine ribonucleotides in which the phosphate residues of each uridine ribonucleotide act as bridges in forming diester linkages between the ribose moieties. Polyuridylic Acids,Uracil Polynucleotides,Poly(rU),Acids, Polyuridylic,Polynucleotides, Uracil
D002701 Chloramphenicol An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106) Cloranfenicol,Kloramfenikol,Levomycetin,Amphenicol,Amphenicols,Chlornitromycin,Chlorocid,Chloromycetin,Detreomycin,Ophthochlor,Syntomycin
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome
D012343 RNA, Transfer The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains. Suppressor Transfer RNA,Transfer RNA,tRNA,RNA, Transfer, Suppressor,Transfer RNA, Suppressor,RNA, Suppressor Transfer
D013752 Tetracycline A naphthacene antibiotic that inhibits AMINO ACYL TRNA binding during protein synthesis. 4-Epitetracycline,Achromycin,Achromycin V,Hostacyclin,Sustamycin,Tetrabid,Tetracycline Hydrochloride,Tetracycline Monohydrochloride,Topicycline,4 Epitetracycline

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