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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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Bibliografske podrobnosti
izdano v:Nucleic Acids Res
Main Authors: Miller, S P, Bodley, J W
Format: Artigo
Jezik:Inglês
Izdano: Oxford University Press 1991
Online dostop: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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