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Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome.

The translocation reaction catalyzed by elongation factor G (EF-G) is inhibited either by alpha-sarcin cleavage of 23S rRNA or by the binding of thiostrepton to the E. coli ribosome. Here we show that the transitory binding of EF-G and GDP to the ribosome inhibited the rate of alpha-sarcin cleavage...

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Detalhes bibliográficos
Main Authors: Miller, S P, Bodley, J W
Formato: Artigo
Idioma:Inglês
Publicado em: 1991
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC333929/
https://ncbi.nlm.nih.gov/pubmed/2027773
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