Abstract

Initiation of Translation is mediated by specific recognition of the cap structure by eukaryotic translation initiation factor 4F (eIF4F), which is a cap binding protein complex that consists of three subunits: eIF4A, eIF4E and eIF4G. We have identified a novel transcription initiation factor (TI-1) in the smooth muscle cells of Gastrointestinal tract of Rabbit using with a forward primer and a reverse primers. Bioinformatics analysis of the PCR product revealed that the sequence is closely related with Homo sapiens eukaryotic translation initiation factor 4 gamma 2 (IEF4g2) splice variant 2 mRNA with 97% homology. Phylogentic analysis revealed this region is closely related with human chromosome 11 location 11p15 with a score of 351 and E value of 8e-95 and the sequence is more correlated to the group of primates with a sequence difference of only 0.75 in the course of evolution by Neighbour joining tree method with a boot strap value of 10000. Structurally observed that this gene closely related to the X-ray strucutre of phylogenetically conserved middle region of human eukaryotic initiation factor (eIF) 4GII revealing a crescent-shaped domain consisting of ten alpha helices arranged as five HEAT repeats. Together with the ATP-dependent RNA helicase eIF4A, this HEAT domain is resposponsible for 48S ribosomal complex formation with a picornaviral RNA internal ribosome entry site.

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