Inhibition of ribosomal A site functions by sporangiomycin and micrococcin.
Sporangiomycin and micrococcin inhibit the binding of aminoacyl-transfer ribonucleic acid into the ribosomal A site in intact bacterial protoplasts. They also prevent the assembly of [ribosome-elongation factor G-guanine nucleotide] complexes in vitro and compete with [(35)S]thiostrepton for ribosomal binding sites. We conclude that micrococcin and sporangiomycin block the ribosomal A site in the vicinity of the complex guanosine triphosphatase center and so resemble thiostrepton in their modes of action.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001410:Bacillus megaterium / Q000378:metabolism / Q000648:ultrastructure; D001430:Bacteriocins; D004926:Escherichia coli / Q000378:metabolism / Q000648:ultrastructure; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides / Q000494:pharmacology; D012329:RNA, Bacterial / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects*; D013883:Thiostrepton / Q000378:metabolism
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D012329:RNA, Bacterial; C009779:micrococcin; C003339:sporangiomycin; D012343:RNA, Transfer; D013883:Thiostrepton