The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.

@article{Schuch2014TheEF,
  title={The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.},
  author={Benjamin Schuch and Monika Feigenbutz and Debora Lika Makino and Sebastian Falk and Claire Basquin and Phil Mitchell and Elena Conti},
  journal={The EMBO journal},
  year={2014},
  volume={33 23},
  pages={2829-46}
}
The exosome is a conserved multi-subunit ribonuclease complex that functions in 3' end processing, turnover and surveillance of nuclear and cytoplasmic RNAs. In the yeast nucleus, the 10-subunit core complex of the exosome (Exo-10) physically and functionally interacts with the Rrp6 exoribonuclease and its associated cofactor Rrp47, the helicase Mtr4 and Mpp6. Here, we show that binding of Mtr4 to Exo-10 in vitro is dependent upon both Rrp6 and Rrp47, whereas Mpp6 binds directly and… CONTINUE READING
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