[2] The prokaryotic initiation factor, IF3, assists with start site specificity, as well as mRNA binding.
IF1 and eIF1A, both containing an OB-fold, bind to the A site and assist in the assembly of initiation complexes at the start codon.
It helps to create the 43S pre-initiation complex, composed of the small 40S subunit attached to other initiation factors.
The eIF3 factor can also be used post-translation in order to separate the ribosomal complex and keep the small and large subunits apart.
[8] Another important eukaryotic initiation factor, eIF2, binds the tRNA containing methionine to the P site of the small ribosome.
[9] In cancerous cells, initiation factors assist in cellular transformation and development of tumors.
The survival and growth of cancer is directly related to the modification of initiation factors and is used as a target for pharmaceuticals.
Some initiation factors, such as eIF4E, are important in synthesizing specific proteins needed for the proliferation and survival of cancer.
Due to its role in creating the 43S pre-initiation complex, it helps to bind the ribosomal subunit to the mRNA.
It is prevalent during early stages of oncogenesis and likely selectively translates proteins needed for cell proliferation.
[8] When eIF3a is suppressed, it has shown to decrease the malignancy of breast and lung cancer, most likely due to its role in tumor growth.