期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 24, 期 5, 页码 453-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3396
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资金
- German Research Council [SFB 902, SFB 646, FOR 1805, GRK 1721]
- Center for Integrated Protein Science Munich (CiPS-M)
- European Research Council
- Cluster of Excellence-Macromolecular Complexes [EXC 115]
- Boehringer Ingelheim
- Leibniz-Rechenzentrum Munich (LRZ)
The essential ATP-binding cassette protein ABCE1 splits 80S ribosomes into 60S and 40S subunits after canonical termination or quality-control-based mRNA surveillance processes. However, the underlying splitting mechanism remains enigmatic. Here, we present a cryo-EM structure of the yeast 40S-ABCE1 post-splitting complex at 3.9-angstrom resolution. Compared to the pre-splitting state, we observe repositioning of ABCE1's iron-sulfur cluster domain, which rotates 150 degrees into a binding pocket on the 40S subunit. This repositioning explains a newly observed anti-association activity of ABCE1. Notably, the movement implies a collision with A-site factors, thus explaining the splitting mechanism. Disruption of key interactions in the post-splitting complex impairs cellular homeostasis. Additionally, the structure of a native post-splitting complex reveals ABCE1 to be part of the 43S initiation complex, suggesting a coordination of termination, recycling, and initiation.
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