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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...

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Detalles Bibliográficos
Autores principales: Cuzic-Feltens, Simona, Weber, Michael H. W., Hartmann, Roland K.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2009
Materias:
RNA
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