Bacillus subtilis RNA deprotection enzyme RppH recognizes guanosine in the second position of its substrates.

@article{Piton2013BacillusSR,
  title={Bacillus subtilis RNA deprotection enzyme RppH recognizes guanosine in the second position of its substrates.},
  author={J{\'e}r{\'e}mie Piton and Val{\'e}ry Larue and Yann Thillier and Audrey Dorl{\'e}ans and Olivier Pellegrini and In{\`e}s Li de la Sierra-Gallay and Jean-Jacques Vasseur and Françoise Debart and Carine Tisn{\'e} and Ciar{\'a}n Condon},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 22},
  pages={
          8858-63
        }
}
The initiation of mRNA degradation often requires deprotection of its 5' end. In eukaryotes, the 5'-methylguanosine (cap) structure is principally removed by the Nudix family decapping enzyme Dcp2, yielding a 5'-monophosphorylated RNA that is a substrate for 5' exoribonucleases. In bacteria, the 5'-triphosphate group of primary transcripts is also converted to a 5' monophosphate by a Nudix protein called RNA pyrophosphohydrolase (RppH), allowing access to both endo- and 5' exoribonucleases… CONTINUE READING

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