Abstract
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.
MeSH Terms
Anti-Bacterial Agents/pharmacology
Bacillus megaterium/metabolism,ultrastructure
Bacteriocins
Escherichia coli/metabolism,ultrastructure
Intercellular Signaling Peptides and Proteins
Peptides/pharmacology
RNA, Bacterial/metabolism
RNA, Transfer/metabolism
Ribosomes/drug effects
Thiostrepton/metabolism
Chemicals
Anti-Bacterial Agents
Bacteriocins
Intercellular Signaling Peptides and Proteins
Peptides
RNA, Bacterial
micrococcin
sporangiomycin
RNA, Transfer
Thiostrepton
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cundliffe E
Dixon P D
References (20)
20 references, click to expand
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