Structure of an AAGU tetraloop and its contribution to substrate selection by yeast RNase III.

@article{Gaudin2006StructureOA,
  title={Structure of an AAGU tetraloop and its contribution to substrate selection by yeast RNase III.},
  author={Cyril Gaudin and Ghada Ghazal and Satoko Yoshizawa and Sherif Abou Elela and Dominique Fourmy},
  journal={Journal of molecular biology},
  year={2006},
  volume={363 2},
  pages={322-31}
}
RNase III enzymes are a highly conserved family of proteins that specifically cleave double-stranded RNA (dsRNA). These proteins are involved in a variety of cellular functions, including the processing of many non-coding RNAs, mRNA decay, and RNA interference. In yeast Rnt1p, a dsRNA-binding domain (dsRBD) recognizes its substrate by interacting with stems capped with conserved AGNN tetraloops. The enzyme uses the tetraloop to cut 14nt to 16nt away into the stem in a ruler-like mechanism. The… CONTINUE READING

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