Chaperone-directed ribosome repair after oxidative damage
Yoon-Mo Yang1, Youngeun Jung2, Daniel Abegg2
1Department of Integrative Structural and Computational Biology, The Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology, Jupiter, FL 33458, USA.
Molecular Cell
|April 22, 2023
Summary
Cells possess a novel ribosome repair pathway. Chaperones remove damaged ribosomal proteins (RPs), allowing ribosome repair, crucial for growth and mitigating oxidative stress effects.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Ribosomes are essential for protein synthesis and quality control.
- Oxidative stress damages cellular components, including ribosomes.
- Mechanisms for repairing damaged ribosomal proteins (RPs) remain unclear.
Purpose of the Study:
- To investigate how cells mitigate damage to ribosomal proteins (RPs).
- To elucidate the role of chaperones in ribosome repair.
- To understand the implications of this pathway for cellular health.
Main Methods:
- Analysis of oxidative damage to specific ribosomal proteins (Rps26, Rpl10).
- Investigating the role of chaperones Tsr2 and Sqt1 in RP removal.
- Assessing the impact of pathway ablation on cell growth under stress.
Main Results:
- Cysteines in Rps26 and Rpl10 are susceptible to oxidative damage, causing dysfunction.
- Chaperones Tsr2 and Sqt1 release damaged RPs, enabling ribosome repair.
- Impairing this repair pathway hinders growth, especially under oxidative stress.
Conclusions:
- A novel chaperone-mediated ribosome repair pathway exists.
- This pathway is vital for maintaining ribosome integrity and cellular function.
- Findings offer insights into aging, health, and previous observations of protein exchange in dendrites.
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