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. 1994 Oct 25;22(21):4449–4453. doi: 10.1093/nar/22.21.4449

Chemical probing of a virginiamycin M-promoted conformational change of the peptidyl-transferase domain.

P Vannuffel 1, M Di Giambattista 1, C Cocito 1
PMCID: PMC308478  PMID: 7971275

Abstract

Previous findings suggest the location of the central loop of domain V of 23S rRNA within the peptidyltransferase domain of ribosomes. This enzymatic activity is inhibited by some antibiotics, including type A (virginiamycin M or VM) and type B (virginiamycin S or VS) synergimycins, antibiotics endowed with a synergistic action in vivo. In the present work, the ability of VM and VS to modify the accessibility of 23S rRNA bases within ribosomes to chemical reagents has been explored. VM afforded a protection of rRNA bases A2037, A2042, G2049 and C2050. Moreover, when ribosomes were incubated with the two virginiamycin components, the base A2062, which was protected by VS alone, became accessible to dimethyl sulphate (DMS). Modified reactivity to chemical reagents of different rRNA bases located either in the central loop of domain V or in its proximity furnishes experimental evidence for conformational ribosome alterations induced by VM binding.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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