Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components
Radioactive carbomycin A, niddamycin, tylosin, and spiramycin, but not erythromycin, can be covalently bound to Escherichia coli ribosomes by incubation at 37 degrees C. The incorporation of radioactivity into the particles is inhibited by SH- and activated double bond containing compounds but not by amino groups, suggesting that the reactions may take place by addition to the double bond present in the reactive antibiotics. This thermic reaction must be different from the photoreaction described for some of these macrolides (Tejedor, F., and Ballesta, J. P. G. (1985) Biochemistry 24, 467-472) since tylosin, which is not photoincorporated, is thermically bound to ribosomes. Most of the radioactivity is incorporated into the ribosomal proteins. Two-dimensional gel electrophoresis of proteins labeled by carbomycin A, niddamycin, and tylosin indicates that about 40% of the radioactivity is bound to protein L27; the rest is distributed among several other proteins such as L8, L2, and S12, to differing extents depending on the drug used. These results indicate, in accordance with previous data, that protein L27 plays an important role in the macrolide binding site, confirming that these drugs bind near the peptidyl transferase center of the ribosome.
- Research Organization:
- Centro de Biologia Molecular, Madrid, Spain
- OSTI ID:
- 6704807
- Journal Information:
- Biochemistry; (United States), Vol. 23
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ANTIBIOTICS
BIOCHEMICAL REACTION KINETICS
CHEMICAL BONDS
ELECTROPHORESIS
ESCHERICHIA COLI
GLYCOSIDES
RIBOSOMES
TRACER TECHNIQUES
ANTI-INFECTIVE AGENTS
BACTERIA
CARBOHYDRATES
CELL CONSTITUENTS
DRUGS
ISOTOPE APPLICATIONS
KINETICS
MICROORGANISMS
ORGANIC COMPOUNDS
ORGANOIDS
REACTION KINETICS
550201* - Biochemistry- Tracer Techniques