Tuteja Renu
Malaria Group; International Centre for Genetic Engineering and Biotechnology; Aruna Asaf Ali Marg, New Delhi, India.
Commun Integr Biol. 2009 May;2(3):245-60. doi: 10.4161/cib.2.3.8843.
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.
真核生物中的蛋白质合成始于多亚基翻译起始复合物eIF4F的结合。该复合物包含eIF4E、eIF4A和eIF4G。eIF4E直接与帽结构相互作用，eIF4A是一种RNA解旋酶，eIF4G作为该复合物的支架。eIF4G包含两个亚基即eIF4A和eIF4E的结合位点，并且它还与聚腺苷酸结合蛋白（PABP）相互作用。在本研究中，我们已经鉴定并表征了恶性疟原虫eIF4F复合物的主要成分，即eIF4E、eIF4A和eIF4G以及PABP。恶性疟原虫eIF4E、eIF4G和PfPABP的分子建模证实它们包含所有特征性的保守结构特征。我们已经注释了恶性疟原虫的一些基因，因此这些研究表明翻译起始复合物的成分高度保守。因此，这些研究将有助于理解恶性疟原虫翻译复合物的基本生物学特性和成分。
