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...
שמור ב:
| הוצא לאור ב: | Nucleic Acids Res |
|---|---|
| Principais autores: | , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
Oxford University Press
1991
|
| גישה מקוונת: | 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 |
| תגים: |
אין תגיות, היה/י הראשונ/ה לתייג את הרשומה!
|