Substrate discrimination in RNase P RNA-mediated cleavage: importance of the structural environment of the RNase P cleavage site

@article{Kikovska2005SubstrateDI,
  title={Substrate discrimination in RNase P RNA-mediated cleavage: importance of the structural environment of the RNase P cleavage site},
  author={Ema Kikovska and Mathias Br{\"a}nnvall and Joanna Kufel and Leif A. Kirsebom},
  journal={Nucleic Acids Research},
  year={2005},
  volume={33},
  pages={2012 - 2021}
}
Like the translational elongation factor EF-Tu, RNase P interacts with a large number of substrates where RNase P with its RNA subunit generates tRNAs with matured 5' termini by cleaving tRNA precursors immediately 5' of the residue at +1, i.e. at the position that corresponds to the first residue in tRNA. Most tRNAs carry a G+1C+72 base pair at the end of the aminoacyl acceptor-stem whereas in tRNA(Gln) G+1C+72 is replaced with U+1A+72. Here, we investigated RNase P RNA-mediated cleavage as a… CONTINUE READING

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