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Investigation of catalysis by bacterial RNase P via LNA and other modifications at the scissile phosphodiester
We analyzed cleavage of precursor tRNAs with an LNA, 2′-OCH(3), 2′-H or 2′-F modification at the canonical (c(0)) site by bacterial RNase P. We infer that the major function of the 2′-substituent at nt −1 during substrate ground state binding is to accept an H-bond. Cleavage of the LNA substrate at...
| Autores principales: | , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Oxford University Press
2009
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2794163/ https://www.ncbi.nlm.nih.gov/pubmed/19793868 http://dx.doi.org/10.1093/nar/gkp775 |