The eIF3 complex is the largest of the eukaryotic initiation factors and is essential for the assembly of the 43S pre-initiation complex. The eIF3j subunit, in particular, is known for its role in modulating mRNA start codon selection . In humans, eIF3j is considered a labile subunit, meaning it can dissociate from the eIF3 complex under certain conditions .
eIF3j has been implicated in several key processes during translation initiation and termination. It facilitates the loading of release factors into the ribosome, which is crucial for translation termination . Specifically, eIF3j stimulates peptidyl-tRNA hydrolysis induced by a complex of eukaryotic release factors, eRF1 and eRF3 . This activity is essential for the proper termination of translation and the release of the newly synthesized polypeptide chain.
The regulation of protein synthesis in eukaryotes predominantly occurs during translation initiation. eIF3, including the eIF3j subunit, is a key regulator of this process. The complex’s ability to modulate start codon selection and facilitate translation termination highlights its importance in maintaining the fidelity and efficiency of protein synthesis .
Research on eIF3j and the eIF3 complex has provided valuable insights into the molecular mechanisms of translation initiation and termination. Studies using model organisms like Neurospora crassa have shown that eIF3 from this fungus is structurally and compositionally similar to human eIF3, making it a useful system for probing the structure and function of human-like eIF3 in living cells .