Structures of CRISPR Cas3 offer mechanistic insights into Cascade-activated DNA unwinding and degradation

@inproceedings{Huo2014StructuresOC,
  title={Structures of CRISPR Cas3 offer mechanistic insights into Cascade-activated DNA unwinding and degradation},
  author={Yanwu Huo and Ki Hyun Nam and Fang Ding and Heejin Lee and Li-jie Wu and Yibei Xiao and F. Daniel Farchione and Sharleen Zhou and Raj Rajashankar and Igor Kurinov and Rongguang Zhang and Ailong Ke},
  booktitle={Nature Structural &Molecular Biology},
  year={2014}
}
CRISPR drives prokaryotic adaptation to invasive nucleic acids such as phages and plasmids, using an RNA-mediated interference mechanism. Interference in type I CRISPR-Cas systems requires a targeting Cascade complex and a degradation machine, Cas3, which contains both nuclease and helicase activities. Here we report the crystal structures of Thermobifida fusca Cas3 bound to single-stranded (ss) DNA substrate and show that it is an obligate 3′-to-5′ ssDNase that preferentially accepts substrate… CONTINUE READING

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CasA mediates Cas3-catalyzed target degradation during CRISPR RNA-guided interference.

Proceedings of the National Academy of Sciences of the United States of America • 2014

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