Abstract
The antibiotic griseoviridin binds to the larger subunit of Escherichia coli ribosomes blocking the interaction between the 3′ terminal end of peptidyl-tRNA and the donor site of the peptidyl transferase centre. Griseoviridin inhibits binding of chloramphenicol, thiamphenicol, lincomycin, erythromycin and streptogramin A to bacterial ribosomes. Moreover griseoviridin protects the ribosomal binding site of gougerotin from the drastic conformational changes taking place in the presence of ethanol. Griseoviridin is also able to interact with eukaryotic ribosomes as shown by its effects on model systems and on anisomycin, trichodermin and gougerotin binding studies. Nevertheless, griseoviridin affinity for the 80-S type ribosomes (yeast or human) is two orders of magnitude smaller than with E. coli ribosomes. The inhibitory spectrum and mode of action of griseoviridin on ribosomes is compared to that of antibiotics of the streptogramin A group and found to be essentially the same.
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