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Title: Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components

Abstract

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.

Authors:
;
Publication Date:
Research Org.:
Centro de Biologia Molecular, Madrid, Spain
OSTI Identifier:
6704807
Resource Type:
Journal Article
Journal Name:
Biochemistry; (United States)
Additional Journal Information:
Journal Volume: 23
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 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

Citation Formats

Tejedor, F, and Ballesta, J P. Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components. United States: N. p., 1986. Web. doi:10.1021/bi00371a066.
Tejedor, F, & Ballesta, J P. Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components. United States. https://doi.org/10.1021/bi00371a066
Tejedor, F, and Ballesta, J P. 1986. "Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components". United States. https://doi.org/10.1021/bi00371a066.
@article{osti_6704807,
title = {Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site components},
author = {Tejedor, F and Ballesta, J P},
abstractNote = {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.},
doi = {10.1021/bi00371a066},
url = {https://www.osti.gov/biblio/6704807}, journal = {Biochemistry; (United States)},
number = ,
volume = 23,
place = {United States},
year = {Tue Nov 18 00:00:00 EST 1986},
month = {Tue Nov 18 00:00:00 EST 1986}
}