Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase J

@inproceedings{Zhao2015StructuralII,
  title={Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase J},
  author={Ye Zhao and Meihua Lu and Hui Min Zhang and Jing Hu and Congli Zhou and Qiang Xu and Amir Miraj Ul Hussain Shah and Hong Xing Xu and Liangyan Wang and Yuejin Hua},
  booktitle={Nucleic acids research},
  year={2015}
}
RNase J is a conserved ribonuclease that belongs to the β-CASP family of nucleases. It possesses both endo- and exo-ribonuclease activities, which play a key role in pre-rRNA maturation and mRNA decay. Here we report high-resolution crystal structures of Deinococcus radiodurans RNase J complexed with RNA or uridine 5'-monophosphate in the presence of manganese ions. Biochemical and structural studies revealed that RNase J uses zinc ions for two-metal-ion catalysis. One residue conserved among… CONTINUE READING
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  • A. Dorleans, I. Li de la Sierra-Gallay, +4 authors C. Condon
  • exo/endoribonuclease RNase J. Structure,
  • 2011
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