PHYLOGENETICS OF ELONGATION FACTOR-G MITOCHONDRIAL PROTEIN GENE (GFM1) IN TEN SELECTED SPECIES
DOI:
https://doi.org/10.51406/jagse.v11i1.1317Keywords:
Elongation factor-G, phylogenetic, protein gene, speciesAbstract
The second stage of protein synthesis is elongation. One of the elongation factors in the elongation cycle of protein synthesis is the elongation factor-G (GFM1). GFM1 is an ancient translational GTPase (trGTPase); the bacterial homolog of eukaryotic eEF2 and archaeal aEF2, respectively. It may interact with the transcriptional apparatus as a positive regulator of RNA synthesis in various species. Genetic variations in GFM1 gene of ten species including cattle, human, chicken, mouse, rat, horse, zebra fish, honeybee, pig and rabbit based on availability were investigated using bioinformatic approach. Using a comparative genomic approach, 4,442 base pairs (bp) of the GFM1 sequences were obtained. Alignment of the sequences within the region of 3,626 bp and containing 816 gaps was carried out using Clustal W software. A very close relationship between rabbit and pig was observed in the phylogenetic tree of GFM1 gene which showed that the comparability of GFM1 gene sequence was highest between the two species and they evolved from a most recent common ancestor with respect to GFM1 gene. Cattle, human, rat and zebra fish were closest by their genetic distances to the ancestor, while mouse, horse, chicken, rabbit and honeybee were distant from the common ancestor. However, close phylogenetic relationship among species might be as a result of conservation of the sequence in the various species.
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References
Alinaghizadeh, R., Mohammad, A.M., Moradnasab, B.S. 2007. Kappa Casein Gene Study in Iranian sistani cattle Breed using PCR-RFLP. Pakistan Journal of Biological Science, 10(23): 4291-4294.
Benjamin, A.P. 2008. Genetics: A Conceptual Approach. Freeman and Company, New York, pp.710.
Farrell, H.M., Jimenez-Florez, R., Bleck, G.T., Brown, E.M., Butler, J.E., Creamer, L.K., Hicks, C.M., Hollar, C. L., Ng-Kwai-Hang, K.F., Swaisgood, H. E. 2004. Nomenclature of the proteins of cows’ milk. Journal of Dairy Science, 87: 1641–1674.
Hirokawa, G., Nijman, R.M., Raj, V.S., Kaji, H., Igarashi, K., Kaji, A. 2005. The role of ribosome recycling factor in dissociation of 70S ribosomes into subunits, RNA, 11:1317-1328.
Tajima, F. 1983. Evolutionary relationship of DNA sequences in finite populations. Genetics, 105: 437-460.
Veerassamy, S., Smith, A., Tillier, E. R. 2003. A transition probability model for amino acid substitutions from Blocks. Journal of Computational Biology, 10: 997-1010.
Zipfel, C., Kunze, G., Chinchilla, D., Caniard, A., Jones, J. D., Boller, T., Felix, G. 2006. Perception of the bacterial PAMP EF-TU by the receptor EFR restricts agrobacterium-mediated transformation. The Cell 125: 749-760.