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Updated: Mar 21, 2026

Preparation and Cryo-FIB micromachining of Saccharomyces cerevisiae for Cryo-Electron Tomography
Published on: November 20, 2021
CryoEM structure of yeast cytoplasmic exosome complex
Jun-Jie Liu1,2, Chu-Ya Niu1, Yao Wu3
1Ministry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
The Ski7 cofactor interacts with the cytoplasmic exosome complex, similar to nuclear Rrp6. RNA binding triggers a switch mechanism, activating the exosome for mRNA degradation through a through-core pathway.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- The eukaryotic RNA exosome complex is essential for RNA processing and decay.
- Ski7 is a key cofactor for the cytoplasmic exosome, targeting mRNAs for degradation.
- The precise interaction of Ski7 with the exosome and RNA substrate processing remains unclear.
Purpose of the Study:
- To elucidate the structural basis of Ski7-exosome interaction.
- To understand the mechanism of RNA substrate processing by the cytoplasmic exosome.
Main Methods:
- Single-particle cryo-electron microscopy (cryo-EM) was employed.
- Structures of the Ski7-exosome complex were determined in both RNA-free and RNA-bound states.
Main Results:
- Cryo-EM structures revealed Ski7's N-terminal domain mimics Rrp6's C-terminal domain interaction with the exosome.
- Analysis of RNA substrates with varying 3' overhangs suggests an RNA-induced activation switch.
- A through-core pathway for RNA processing by the exosome is supported.
Conclusions:
- The study provides the first structural insights into the Ski7-exosome complex.
- A novel RNA-induced activation mechanism for the exosome in mRNA turnover is proposed.
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