Protein synthesis is a fundamental process in cells, with ribosomes playing a crucial role as the cell’s “protein factories.” Ribosomes read the genetic information encoded in messenger RNA (mRNA) and use it to synthesize proteins. These complex molecules consist of two subunits, with the small subunit responsible for reading the mRNA and the large subunit for protein synthesis. It is essential to regulate the production and turnover of ribosomes to ensure efficient protein synthesis in cells.

While the assembly of ribosomes has been extensively studied, the process of ribosomal degradation has remained elusive. In stress situations, such as nutrient deprivation or the stationary phase of cell growth, cells need to reduce their metabolic activity to survive longer. During this phase, some ribosomes are degraded to release energy invested in them. The researchers from the Department of Chemistry at the Universität Hamburg focused on understanding the mechanism of ribosomal degradation in Bacillus subtilis, a common soil bacterium.

Previous studies have identified enzymes like ribonuclease R (RNase R) in the ribosomal degradation process under stress conditions. In this study, researchers used cryo-electron microscopy to visualize how RNase R interacts with the ribosomal 30S subunit. They discovered that RNase R binds to a specific region on the subunit called the “neck” and initiates a two-stage process of degradation. The enzyme destabilizes the neck area in the first stage, making it more flexible, and then turns the head of the subunit in the second stage to continue the degradation process.

Dr. Helge Paternoga, the last author of the study, emphasized the importance of studying cells in the growth phase to understand the transition to the stationary phase. The researchers found that the interaction of RNase R with the 30S subunit was a crucial step in the degradation process. Prof. Dr. Daniel Wilson, the head of the research group, highlighted that RNase R alone could accomplish the complete degradation of the 30S subunit, with the “head” switch being a significant kinetic barrier.

The identification of the dynamic mechanism used by RNase R to degrade ribosomal subunits provides valuable insights into the regulation of protein synthesis and cell survival. Understanding how cells control ribosomal turnover in response to stress conditions can have implications for various fields, including biotechnology and medicine. Further research into the mechanisms of ribosomal degradation could lead to the development of novel therapeutic strategies targeting protein synthesis in cells.

The research team’s discovery of the intricate process of ribosomal degradation by RNase R sheds light on a critical aspect of cellular biology. By unraveling the molecular details of this mechanism, scientists can deepen their understanding of how cells adapt to stress and regulate protein synthesis. The study opens up new avenues for exploring the role of ribosomal degradation in cellular function and may pave the way for future advancements in biotechnology and medicine.


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