Structural basis for processivity and single-strand specificity of RNase II.

@article{Zuo2006StructuralBF,
  title={Structural basis for processivity and single-strand specificity of RNase II.},
  author={Yuhong Zuo and Helen A. Vincent and Jianwei Zhang and Yong Wang and Murray P. Deutscher and Arun Malhotra},
  journal={Molecular cell},
  year={2006},
  volume={24 1},
  pages={149-56}
}
RNase II is a member of the widely distributed RNR family of exoribonucleases, which are highly processive 3'-->5' hydrolytic enzymes that play an important role in mRNA decay. Here, we report the crystal structure of E. coli RNase II, which reveals an architecture reminiscent of the RNA exosome. Three RNA-binding domains come together to form a clamp-like assembly, which can only accommodate single-stranded RNA. This leads into a narrow, basic channel that ends at the putative catalytic center… CONTINUE READING

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