title: Components of the macrolide binding site on the ribosome.
abstract: Carbomycin A, niddamycin and tylosin, macrolide antibiotics that inhibit ribosomal activity, have alpha-beta unsaturated ketone groups in their structure that make them photoreactive. These drugs can also take part in thermic reactions, probably through an addition mechanism to the double bond. Given of the photoactivity and thermic reactivity of their molecules, affinity labeling of the macrolide binding site on the ribosome has been performed using radioactive derivatives of these drugs. After either irradiating or incubating samples containing antibiotics and ribosomal particles, radioactivity appears covalent associated to the proteins. Ribosomal protein L27 is the major labeled component, indicating that this polypeptide, which seems to be part of the peptidyl transferase centre of the ribosome, also plays an important role on the macrolide binding site.
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D006027:Glycosides / Q000378:metabolism; D007700:Kinetics; D007933:Leucomycins / Q000378:metabolism; D018942:Macrolides; D012269:Ribosomal Proteins / Q000302:isolation & purification / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D013329:Structure-Activity Relationship; D015645:Tylosin
chemical_list: D000900:Anti-Bacterial Agents; D006027:Glycosides; D007933:Leucomycins; D018942:Macrolides; D012269:Ribosomal Proteins; C012454:niddamycin; D015645:Tylosin