A research team from the Department of Chemistry at the Universität Hamburg has succeeded for the first time in identifying at the molecular level the dynamic mechanism used by the enzyme RNase R to degrade the ribosomal 30S subunit. The results of the study were published in the scientific journal Nature.
Protein synthesis is a vital and energy-intensive process in the cell in which ribosomes play a crucial role. These comparatively large molecules are found in all living organisms and act as the cell’s “protein factories.”
To do this, ribosomes read the blueprint for a specific protein on a messenger molecule—the messenger RNA (mRNA)—and then convert this information into a new protein. Ribosomes consist of two subunits. The small subunit is responsible for reading and checking the mRNA for errors, while the large subunit is responsible for the polymerization of amino acids to form proteins.
Controlled production and regulated turnover of ribosomes is required for protein synthesis. While the assembly of ribosomes has been increasingly better understood in recent years, there has been no structural insight into the degradation of ribosomes.
This is important because in stress situations such as a lack of food, or at the end of their growth cycle, cells reduce their metabolism in order to survive longer. This state is known as the stationary phase. During this phase,