EIF1AX is a component of the 43S pre-initiation complex (43S PIC), which is essential for the initiation of translation. The 43S PIC binds to the mRNA cap-proximal region, scans the mRNA 5’-untranslated region, and locates the initiation codon . EIF1AX enhances the formation of the cap-proximal complex and, together with EIF1, facilitates scanning, start codon recognition, and the promotion of the assembly of the 48S complex at the initiation codon . This process is crucial for the accurate selection of the start codon and the initiation of protein synthesis.
After the start codon is located, EIF1AX, together with EIF5B, orients the initiator methionine-tRNA in a conformation that allows the joining of the 60S ribosomal subunit to form the 80S initiation complex . This step is vital for the proper assembly of the ribosome and the commencement of translation.
EIF1AX is essential for the binding of the 43S complex (comprising a 40S subunit, eIF2/GTP/Met-tRNAi, and eIF3) to the 5’ end of capped RNA . This binding is a critical step in the initiation of translation, as it ensures that the ribosome is correctly positioned to start protein synthesis. The accurate initiation of translation is fundamental for the proper expression of genes and the production of functional proteins.
Mutations in the EIF1AX gene have been associated with various diseases, including differentiated thyroid carcinoma and thrombocythemia 1 . These mutations can disrupt the normal function of the EIF1AX protein, leading to aberrant translation initiation and the development of disease. Understanding the role of EIF1AX in translation initiation can provide insights into the molecular mechanisms underlying these diseases and potentially lead to the development of targeted therapies.
Recombinant EIF1AX protein is widely used in research to study the mechanisms of translation initiation and the role of EIF1AX in this process. By using human recombinant EIF1AX, researchers can investigate the protein’s function in a controlled environment and gain insights into its interactions with other components of the translation machinery.