2i2O Abstract

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Translation is important in expressing different genes in every cell of every organism. The evolution of eukaryotic organisms meant the need for a more complicated translation structure. An important part of initiating translation in eukaryotes is the eIF4G protein domain. The exact function of this domain and the proteins it encodes for is still not fully understood. This domain contains three identified smaller domains that all encode proteins that have specific functions in intiating translation and binding mRNA. The midddle domain was first isolated from the zebrafish Danio rerio. It was found to be homologous to the middle domain of the eIF4G domain protein in humans. This particular domain, the MIF4G, has had little research conducted on its role in initiation of the eIF4G domain. Computational tools such as Blast, ClustalX, Phylip, ProFunc, Interpro, Nest, Cleft Analysis, PDF database, ProKnow, Pfam and Dali Server were used to determine this particular protein's structure, function and evolutionary history. The MIF4G protein was found to have a wide distribution in a variety of cells such as brain cells, liver cells and kidney cells. This indicates that it has a very important function. MIF4G was found to be important in binding eIF4A, eIF3, RNA and DNA. It was found to be part of the eukaryotic initition factor eIF4G. Its importance in initiating translation affects the type of structure displayed by MIF4G. The domain protein was found to contain many alpha helicases. These are easier to incorporate into novel domains. A phylogenetic tree of 54 sequences closest in alignment to MIF4G was constructed with bootstrap values. The tree constructed only had sequences from multicellular animals. It did not contain sequences from either of the two other major eukaryotic families, plants and fungi.

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