Phylogenetic Analysis of Vacuolar-Type ATPase Proton Pump: V0 Subunit A Isoforms

Authors

  • Shagufta Shafique Department of Bioinformatics, Quaid-e-Azam University, Islamabad, Pakistan
  • Iqra Zafar Department of Biosciences, COMSATS Institute of Information Technology, Sahiwal Pakistan
  • Tooba Iqbal Department of Biosciences, COMSATS Institute of Information Technology, Sahiwal Pakistan
  • Mehreen Zaka Department of Biotechnology, Quaid-i-Azam University Islamabad, Pakistan

Abstract

V-ATPases proton translocating proteins are member of ubiquitous heteromultimeric enzyme family. They couple the ATP energy during various transport processes due to their localization in miscellaneous membranes of eukaroytes. Since, their malfunction is correlated with various diseases in humans, the elucidation of the properties of analyzed enzyme and better understanding into its evolutionary patterns in vertebrates has significance. V-ATPase enzyme consists of Vo and V1 domains, which are further divided into various subunits depending on the type of function and localization. Protein sequences for Vo subunits A of V-ATPase of thirty-four species including vertebrates and invertebrates were extracted and used for the construction of Phylogenetic tree. Analysis of results showed that, Vo subunit A isoform A1 and A4 are highly conserved in vertebrates having high evolutionary constraints whereas isoforms A2 and A3 are fast evolving and under positive selection pressure. Duplication and number of isoforms present in a specie increases with increase in the complexity and cell-specific function and regulation.

Keywords: V-ATPase, V0 domain, Proton pump, Phylogenetic analysis, Gene duplication

Cite this Article

Shagufta Shafique, Iqra Zafar, Tooba Iqbal, Mehreen Zaka, Phylogenetic Analysis of Vacuolar-Type ATPase Proton Pump: V0 Subunit A Isoforms. Research and Reviews: Journal of Computational Biology (RRJoCB). 2015; 4(2): 13–20p.

 

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Published

2015-07-04

Issue

Vol. 4 No. 2 (2015)

Section

Research/Review Articles

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