Functional coupling between a distal interaction and the cleavage site in bacterial RNase-P-RNA-mediated cleavage.

@article{Wu2011FunctionalCB,
  title={Functional coupling between a distal interaction and the cleavage site in bacterial RNase-P-RNA-mediated cleavage.},
  author={Shiying Wu and Yu Chen and Magnus Lindell and Guanzhong Mao and Leif A. Kirsebom},
  journal={Journal of molecular biology},
  year={2011},
  volume={411 2},
  pages={
          384-96
        }
}
Bacterial RNase P consists of one protein and one RNA [RNase P RNA (RPR)]. RPR can process tRNA precursors correctly in the absence of the protein. Here we have used model hairpin loop substrates corresponding to the acceptor, T-stem, and T-loop of a precursor tRNA to study the importance of the T-loop structure in RPR-alone reaction. T-stem/loop (TSL) interacts with a region in RPR [TSL binding site (TBS)], forming TSL/TBS interaction. Altering the T-loop structure affects both cleavage site… CONTINUE READING
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