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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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Detalles Bibliográficos
Publicado en:Nucleic Acids Res
Main Authors: Schlegl, J, Fürste, J P, Bald, R, Erdmann, V A, Hartmann, R K
Formato: Artigo
Idioma:Inglês
Publicado: Oxford University Press 1992
Acceso en liña: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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