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...
Tallennettuna:
| Julkaisussa: | Nucleic Acids Res |
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| Päätekijät: | , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Oxford University Press
1991
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| Linkit: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC333929/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2027773/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/19.7.1657 |
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