RESUMEN

The binding site and probable site of action have been determined for the universal antibiotic amicetin which inhibits peptide bond formation. Evidence from in vivo mutants, site-directed mutations and chemical footprinting all implicate a highly conserved motif in the secondary structure of the 23S-like rRNA close to the central circle of domain V. We infer that this motif lies at, or close to, the catalytic site in the peptidyl transfer centre. The binding site of amicetin is the first of a group of functionally related hexose-cytosine inhibitors to be localized on the ribosome.

Asunto(s)

Antibacterianos/farmacología , Halobacterium salinarum/genética , ARN Ribosómico 23S/genética , Antibacterianos/metabolismo , Secuencia de Bases , Secuencia Conservada , Farmacorresistencia Microbiana/genética , Escherichia coli/efectos de los fármacos , Halobacterium salinarum/metabolismo , Datos de Secuencia Molecular , Conformación de Ácido Nucleico , Mutación Puntual , Biosíntesis de Proteínas/efectos de los fármacos , Nucleósidos de Pirimidina/metabolismo , Nucleósidos de Pirimidina/farmacología , ARN Ribosómico 23S/metabolismo