AsianScientist (Feb. 13, 2026) – Ribosomes are the protein factories of our cells, translating messenger RNA (mRNA) into amino acids to synthesise the many proteins that sustain our bodies.
Responsible for a wide range of functions, proteins catalyse biochemical reactions, act as chemical messengers, and form structures (including ribosomes) to make up our bodies.
Since proteins are so important, it is vital that ribosomes function efficiently and accurately. Until now, scientists have not understood how cells can detect inefficient ribosomes.
A team of researchers from the University of Tokyo and Tohoku University have identified a quality control mechanism by which cells mark less efficient ribosomes for removal. Published in Nature Communications, this study found that less efficient ribosomes are selectively removed when there are better ribosomes present in the cell.
The researchers engineered yeast cells to contain an additional, suboptimal ribosome variant that moves more slowly than the native ribosomes in the cell. They then used biochemical and genetic analyses to examine the effect of disrupted translation carried out by the suboptimal ribosomes.
Ribosomes work by travelling along a string of mRNA as they ‘read’ it, translating each codon into a corresponding amino acid. When ribosomes in the yeast cells translated the same strand of messenger RNA, the slower, suboptimal ribosomes were overtaken by the native ribosomes, causing the two to collide
“Ribosome collisions act like a cellular warning signal,” said Assistant Professor Sihan Li, lead author of the paper. “When ribosomes bump into each other, it alerts the cell that something is wrong. The cell then removes the problematic ribosomes to maintain efficient protein production.”
The colliding ribosomes activate a quality control pathway that triggers ubiquitination. A small protein called ubiquitin attaches to one of the proteins that make up the ribosome, marking it for degradation or quality control.
“Our study introduces the concept of ribosome competition, showing that even functional but slower ribosomes are selectively degraded when more capable ones are available,” said Dr Li. “It is fascinating to see how cells apply a principle similar to survival of the fittest at the molecular level.”
The researchers also explored the effects of cisplatin on the ribosome quality control process. Cisplatin is a widely used cancer drug that interacts with genetic material, so the scientists hypothesised that this might disrupt ribosome dynamics by linking different RNA types together.
Cisplatin was found to increase ribosome collisions, thus activating the ubiquitination pathway and increasing the rate of ribosome degradation. This could help explain some of cisplatin’s side effects, and improves our understanding of the drug’s toxicity and efficacy.
These results provide insight into the quality control process for ribosomes, and could help us understand disorders caused by ribosome malfunctions (ribosomopathies). As seen with cisplatin, this may also open new approaches to improve the effectiveness of some drugs.
“We hope people find it interesting that even at the microscopic level, competition drives quality and resilience,” said Dr. Li. “This discovery connects a fundamental evolutionary idea to the inner workings of our cells.”
—
Source: University of Tokyo;Image:Steven McDowell/Shutterstock
This article can be found at: Collision-induced ribosome degradation driven by ribosome competition and translational perturbations
Disclaimer: This article does not necessarily reflect the views of AsianScientist or its staff.
