Journal
SCIENCE
Volume 360, Issue 6385, Pages 219-222Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar5428
Keywords
-
Categories
Funding
- Max Planck Gesellschaft E.C
- European Commission (ERC Advanced Investigator Grant EXORICO)
- European Commission (ERC Advanced Investigator Grant Glowsome)
- Deutsche Forschungsgemeinschaft [DFG SFB646, SFB1035, GRK1721, HU363/10-5, HU363/12-1]
- Deutsche Forschungsgemeinschaft (CIPSM)
- Louis Jeantet Foundation
Ask authors/readers for more resources
The RNA exosome complex processes and degrades a wide range of transcripts, including ribosomal RNAs (rRNAs). We used cryo-electron microscopy to visualize the yeast nuclear exosome holocomplex captured on a precursor large ribosomal subunit (pre-60S) during 7S-to-5.8S rRNA processing. The cofactors of the nuclear exosome are sandwiched between the ribonuclease core complex (Exo-10) and the remodeled foot structure of the pre-60S particle, which harbors the 5.8S rRNA precursor. The exosome-associated helicase Mtr4 recognizes the preribosomal substrate by docking to specific sites on the 25S rRNA, captures the 3' extension of the 5.8S rRNA, and channels it toward Exo-10. The structure elucidates how the exosome forms a structural and functional unit together with its massive pre-60S substrate to process rRNA during ribosome maturation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available