Ribosomes, comprising the 40S (small subunit) and 60S (large subunit) in eukaryotes, are essential for cellular protein synthesis, often referred to as translation. The 40S and 60S subunits collectively contain four different types of RNA and around 80 unique proteins, each with distinct structural features. They function by decoding messenger RNA (mRNA) sequences and catalyzing the synthesis of polypeptides, the building blocks of proteins. The 40S subunit is responsible for the binding and reading of mRNA, while the 60S subunit facilitates the formation of peptide bonds between amino acids. This process is highly regulated and involves various stages: initiation, elongation, termination, and ribosome recycling. Ribosomes are also involved in controlling the rate of protein synthesis, which is crucial for maintaining cellular homeostasis and responding to environmental cues. Malfunction or alterations in ribosomal function can lead to various cellular issues, often resulting in diseases known as ribosomopathies.
Targeting ribosomes and their function for disruption or inhibition using small molecules is a powerful strategy for understanding the mechanisms of protein synthesis. Small molecule inhibitors can bind to specific sites on the ribosome, revealing key interactions and structural features essential for its function. By inhibiting different stages of translation – such as initiation, elongation, or termination – these compounds help in dissecting the precise steps and factors involved in protein synthesis. This approach is crucial for studying how ribosomes interpret genetic information and assemble amino acids into proteins, a fundamental process in all living cells. Additionally, observing the effects of ribosomal inhibitors on cellular processes provides insights into how disruptions in protein synthesis can lead to various diseases.