Cleavage efficiencies of model substrates for ribonuclease P from Escherichia coli and Thermus thermophilus.
We compared cleavage efficiencies of mono-molecular and bipartite model RNAs as substrates for RNase P RNAs (M1 RNAs) and holoenzymes from E. coli and Thermus thermophilus, an extreme thermophilic eubacterium. Acceptor stem and T arm of pre-tRNA substrates are essential recognition elements for both...
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| Опубликовано в:: | Nucleic Acids Res |
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| Главные авторы: | , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
Oxford University Press
1992
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| Online-ссылка: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC334461/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1281315/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/20.22.5963 |
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