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-Structure paper
| Title | Structure of the nuclear exosome captured on a maturing preribosome. |
|---|---|
| Journal, issue, pages | Science, Vol. 360, Issue 6385, Page 219-222, Year 2018 |
| Publish date | Apr 13, 2018 |
 Authors | Jan Michael Schuller / Sebastian Falk / Lisa Fromm / Ed Hurt / Elena Conti /  |
| PubMed Abstract | 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 ...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-60) during 7-to-5.8 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-60 particle, which harbors the 5.8 rRNA precursor. The exosome-associated helicase Mtr4 recognizes the preribosomal substrate by docking to specific sites on the 25 rRNA, captures the 3' extension of the 5.8 rRNA, and channels it toward Exo-10. The structure elucidates how the exosome forms a structural and functional unit together with its massive pre-60 substrate to process rRNA during ribosome maturation. |
 External links | Science / PubMed:29519915 |
| Methods | EM (single particle) |
| Resolution | 3.9 - 4.6 Å |
| Structure data | |
| Chemicals |  ChemComp-ZN:  ChemComp-GTP:  ChemComp-MG: |
| Source |
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 Keywords |  RNA / RNA exosome / Ribosome / pre-ribosome / Mtr4 / Helicase |
