Determinants in the rpsT mRNAs recognized by the 5'-sensor domain of RNase E.

@article{Mackie2013DeterminantsIT,
  title={Determinants in the rpsT mRNAs recognized by the 5'-sensor domain of RNase E.},
  author={George A. Mackie},
  journal={Molecular microbiology},
  year={2013},
  volume={89 2},
  pages={
          388-402
        }
}
RNase E plays a central role in processing virtually all classes of cellular RNA in many bacterial species. A characteristic feature of RNase E and its paralogue RNase G, as well as several other unrelated ribonucleases, is their preference for 5'-monophosphorylated substrates. The basis for this property has been explored in vitro. At limiting substrate, cleavage of the rpsT mRNA by RNase E (residues 1-529) is inefficient, requiring excess enzyme. The rpsT mRNA is cleaved sequentially in a 5… CONTINUE READING
BETA