Eukaryotic Translation Initiation Factor 3 (eIF3) is a multiprotein complex essential for the initiation phase of eukaryotic translation. It plays a crucial role in the formation of the preinitiation complex (PIC) and the recruitment of mRNA to the ribosome. Among its subunits, eIF3I is a significant component that contributes to the overall function of the eIF3 complex.
The eIF3 complex in humans consists of 13 nonidentical subunits (eIF3a-m) with a combined molecular weight of approximately 800 kDa, making it the largest translation initiation factor . The eIF3I subunit is a single, non-glycosylated polypeptide chain containing 348 amino acids and has a molecular mass of 38.9 kDa . It is often produced recombinantly in E. coli or Sf9 Baculovirus cells for research purposes .
eIF3I, along with other subunits of the eIF3 complex, is involved in various steps of translation initiation. The eIF3 complex binds to the small ribosomal subunit (40S) and serves as a scaffold for several other initiation factors, including eIF1, eIF1A, eIF2, and eIF5 . This binding facilitates the formation of the 43S preinitiation complex (PIC), which is essential for the recruitment of mRNA and the scanning of the mRNA leader sequence for the start codon .
The eIF3 complex, including eIF3I, plays a pivotal role in the initiation of translation by:
Recombinant eIF3I is widely used in research to study the mechanisms of translation initiation and the role of individual subunits in this process. Structural studies, such as cryo-electron microscopy (cryo-EM), have provided insights into the interactions between eIF3I and other components of the translation machinery . Additionally, recombinant eIF3I is used to investigate its potential role in various diseases and to develop therapeutic interventions targeting translation initiation.