Abstract
Protein synthesis in eukaryotes initiates with binding of the multisubunit translation initiation complex eIF4F. This complex contains eIF4E, eIF4A and eIF4G. eIF4E directly interacts with the cap structure, eIF4A is an RNA helicase and eIF4G acts as a scaffold for the complex. eIF4G contains the binding sites for both the subunits i.e., eIF4A and eIF4E and it also interacts with poly(A)-binding protein (PABP). In present study we have identified and characterized the main components of the eIF4F complex i.e., eIF4E, eIF4A and eIF4G and PABP from Plasmodium falciparum. Molecular modeling of PfeIF4E, PfeIF4G and PfPABP confirms that they contain all the characteristic conserved structural features. We have annotated some of the genes of P. falciparum and as a result these studies demonstrate that the components of translation initiation complex are highly conserved. Therefore these studies will contribute to understand the basic biology and components of translation complex in P. falciparum.