Molecular evolution study of vertebrate rps27 homologues

• Main Author: Tiong, Patrick Joon Kiat.
• Format: E-LPTA
• Language: English; English
• Published: unimas 2010
• Subjects: Q Science (General); QK Botany
• Online Access: http://ir.unimas.my/id/eprint/20792/1/Molecular%20evolution%20study%20of%20vertebrate%20RPS27%20homologues%20%2824%20pgs%29.pdf; http://ir.unimas.my/id/eprint/20792/2/Molecular%20evolution%20study%20of%20vertebrate%20RPS27%20homologues.pdf; http://ir.unimas.my/id/eprint/20792/

RPS27 is a protein coding gene that constitutes one of the components in small ribosomal subunit and its housekeeping funŸtion makes RPS27 gene likely to be expressed in every cells types of all living organisms. It has unique Zinc finger like structure that have been deduced potentially function to bind and interact with nucleic acids. In this study, multiple sequence alignment of protein coding sequence and phylogenetic analysis were carried out to delineate the substitution pattern and the evolutionary relationship of the RPS27 homologues sequence among vertebrates. High similarity from multiple sequence alignment and protein secondary structure of the RPS27 and RPS27L genes which located in different genome location have lead to the possibility that RPS27 have undergo gene duplication during divergence of the vertebrates species and both sharing orthologs and paralogs relationships. However, the exact divergence time of RPS27 homologue are not investigated in this study. Besides that, this research also revealed that RPS27 homologous are highly conserved in the amino acids sequence and therefore reflected strict selective pressure acting on the homologues sequences to maintain indigenous functionality of the protein. Further evolutionary functionality of the protein also have been investigated, suggesting that acidic and aliphatic amino acids residue flanking the clustered basic amino acid residues have evolved in the vertebrates RPS27 proteins may facilitate the appropriate orientation of the nucleic acids from interaction with the nuclear localisation signal towards Zinc finger structure of RPS27 protein.