Ribosomal Protein L22, Epstein-Barr-Encoded RNA-Associated Protein, Epstein-Barr Virus Small RNA-Associated Protein, 60S Ribosomal Protein L22, EBER-Associated Protein, EAP, HBP15/L22.
Ribosomal Protein L22, Epstein-Barr-Encoded RNA-Associated Protein, Epstein-Barr Virus Small RNA-Associated Protein, 60S Ribosomal Protein L22, EBER-Associated Protein, EAP, HBP15/L22.
Ribosomal Protein L22 (RPL22) is a component of the large 60S subunit of the ribosome, which plays a crucial role in protein synthesis. Ribosomes are essential macromolecular machines within the cell, responsible for translating mRNA into functional proteins. RPL22 is one of the many ribosomal proteins that contribute to the structure and function of the ribosome.
RPL22 is an external protein on the 60S ribosomal subunit that is incorporated into the ribosome at later stages of ribosome maturation . It has a highly conserved structure across different species, indicating its essential role in ribosome function. The protein is involved in the assembly and stability of the ribosome, ensuring accurate translation of genetic information.
Recent studies have suggested that ribosomal proteins, including RPL22, may have regulatory functions beyond their structural roles. For instance, RPL22 has been shown to control the composition of the ribosome by directly repressing the expression of its own paralog, RPL22-like1 (RPL22L1) . This regulation is achieved through binding to an internal hairpin structure in the mRNA of RPL22L1, thereby influencing its expression and incorporation into ribosomes.
Human recombinant RPL22 is produced using recombinant DNA technology, which involves inserting the gene encoding RPL22 into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the protein for research and therapeutic purposes. Recombinant RPL22 retains the same structure and function as the naturally occurring protein, making it a valuable tool for studying ribosome biology and potential therapeutic applications.
Mutations in ribosomal proteins, including RPL22, have been linked to various human diseases. These include developmental malformations, inherited bone marrow failure syndromes, and cancer . Understanding the role of RPL22 in ribosome function and its regulatory mechanisms can provide insights into the molecular basis of these diseases and potential therapeutic targets.