Eukaryotic Translation Initiation Factor 4E (eIF4E) is a crucial protein involved in the initiation of translation in eukaryotic cells. It is a part of the eIF4F complex, which plays a pivotal role in the recognition of the 5’ cap structure of messenger RNAs (mRNAs) and the recruitment of ribosomes to initiate protein synthesis . The human recombinant form of eIF4E is produced using recombinant DNA technology, allowing for its use in various research and therapeutic applications.
eIF4E is a cap-binding protein that specifically recognizes and binds to the 7-methylguanosine (m7G) cap at the 5’ end of eukaryotic mRNAs . This binding is essential for the recruitment of the eIF4F complex, which includes eIF4A (a helicase) and eIF4G (a scaffolding protein) . The eIF4F complex facilitates the unwinding of secondary structures in the 5’ untranslated region (UTR) of the mRNA, allowing the ribosome to access the mRNA and initiate translation .
eIF4E is a rate-limiting factor in cap-dependent translation, meaning its availability and activity directly influence the efficiency of protein synthesis . It is involved in various cellular processes, including cell growth, proliferation, and survival . Dysregulation of eIF4E has been implicated in several diseases, including cancer, where its overexpression is often associated with tumorigenesis and poor prognosis .
The human recombinant form of eIF4E is produced using recombinant DNA technology, typically in bacterial or yeast expression systems . This involves cloning the eIF4E gene into an expression vector, transforming the host cells, and inducing protein expression. The recombinant protein is then purified using affinity chromatography techniques, such as His-tag or GST-tag purification .
Recombinant eIF4E is widely used in research to study the mechanisms of translation initiation and its regulation . It is also used in drug discovery and development, particularly in the search for inhibitors that can modulate eIF4E activity for therapeutic purposes . Additionally, recombinant eIF4E can be used in structural biology studies to elucidate its interactions with other components of the translation machinery .