Open AccessInteraction of the antibiotic sparsomycin with the ribosome
Author(s) -
Ester Lázaro,
Ana SanFélix,
L.A.M. van den Broek,
H. C. J. Ottenheijm,
Juan P. G. Ballesta
Publication year - 1991
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.35.1.10
Subject(s) - ribosome , rnase p , peptidyl transferase , chemistry , a site , chloramphenicol , tetracycline , protein biosynthesis , biochemistry , antibiotics , stereochemistry , binding site , biophysics , rna , biology , gene
Phenol-alanine-sparsomycin, a derivative of sparsomycin carrying a p-hydroxy-benzyl function easily labeled by iodination, has been used to study the interaction of this drug with the ribosome. Our study indicated that the binding of the drug to the ribosome is sensitive to trichloracetic acid and is equally affected by disintegration of the particle after RNase and protease treatments. The ribosome is not irreversibly inactivated, and the chemical structure of the drug is not affected by interaction with the particle. These data are not compatible with the proposed covalent association of sparsomycin with the ribosome by G. A. Flynn and R. J. Ash (Biochem. Biophys. Res. Commun. 114:1-7, 1983); therefore, the antibiotic must inhibit protein synthesis through a reversible interaction with the ribosome.