Mitochondrial ribosomes, also known as mitoribosomes, are responsible for protein synthesis within the mitochondria. They consist of a small 28S subunit and a large 39S subunit. Unlike prokaryotic ribosomes, which have a higher rRNA to protein ratio, mitoribosomes have an estimated 75% protein to rRNA composition . This difference is significant because it highlights the unique evolutionary path of mitochondrial ribosomes compared to their prokaryotic counterparts.
The MRPS23 protein itself is composed of 190 amino acids and has a calculated molecular mass of approximately 21.8 kDa . It plays a crucial role in the assembly and function of the mitochondrial ribosome, contributing to the overall process of mitochondrial protein synthesis.
Mutations or deficiencies in the MRPS23 gene have been associated with certain mitochondrial disorders. Notably, Combined Oxidative Phosphorylation Deficiency 46 and Combined Oxidative Phosphorylation Deficiency 8 are linked to anomalies in this gene . These conditions can lead to severe metabolic dysfunctions due to impaired mitochondrial protein synthesis.
The proteins comprising the mitoribosome, including MRPS23, differ significantly in sequence and biochemical properties among different species . This variability prevents easy recognition by sequence homology and underscores the evolutionary divergence of mitochondrial ribosomes from their prokaryotic ancestors.
Research on MRPS23 and other mitochondrial ribosomal proteins is ongoing, with a focus on understanding their roles in mitochondrial function and their implications in various diseases. Recombinant forms of MRPS23 are used in research to study its structure, function, and interactions with other mitochondrial components.