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Updated: Apr 21, 2026

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC
Published on: May 9, 2020
rRNA expansion segments mediate ribosome dimerization as a conserved stress response
Wenhong Jiang1,2, Chen Chen1,3, Xing Wang1
1State Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, School of Life Sciences, Peking University, Beijing 100871, China.
Puromycin triggers ribosome hibernation in cells, forming idle dimeric complexes. This conserved mechanism protects ribosomes during cellular stress, revealing new insights into translation regulation.
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- Inhibition of messenger RNA translation is a key cellular response to proteostatic stress.
- Puromycin disrupts protein synthesis and is used to study translation, but its cellular effects are not fully understood.
Purpose of the Study:
- To investigate the in situ effects of puromycin on the translation machinery.
- To elucidate the cellular response to puromycin-induced translation stress.
Main Methods:
- Electron tomography
- Topology analysis
- In situ structural analysis of ribosomes
Main Results:
- Puromycin treatment leads to accumulation of eIF5A-bound ribosomes in an inactive 'idle' state.
- Idle ribosomes form dimeric complexes via ribosomal RNA expansion segments, suggesting a hibernation mechanism.
- Disome formation is a conserved response to various cellular stressors, including ER stress and amino acid depletion.
Conclusions:
- Puromycin induces distinct states of mammalian ribosome hibernation and dimerization.
- Ribosomal RNA expansion segments play a role in ribosome hibernation and protection.
- Ribosome hibernation is a conserved cellular response to diverse stress conditions, impacting ribosomal activity regulation.
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