F1FoATP synthase a-subunit of Stenotrophomonas sp. DL18 from Indian Soda Lake, Lonar: a brief report

Devendra Lingojwar,Kachru Gawai,Ravikant Jadhav

doi:10.12688/f1000research.1-62.v1

Abstract

Lonar Lake, an Indian Soda Lake, is well known for its biodiversity of extremophiles including alkaliphiles. Most of the molecular studies on Lonar Lake alkaliphiles are based on molecular identification by 16S ribosomal RNA along with numerous applications in the biotechnology industry. However, molecular basis of adaptation of these alkaliphiles to high alkaline conditions is incompletely understood. Attempts were made to isolate and identify alkaliphiles from their naturally occurring original habitat, i.e. Lonar Lake, India with high alkaline conditions of pH 10.5. One facultative alkaliphile,Stenotrophomonasspecies DL18, was studied for F1FoATP synthase a-subunit with reference to alkaliphile-specific domains. Although the a-subunit ofStenotrophomonasDL18 showed significant similarity with neutrophiles, the isolated bacterium is an alkaliphile and optimally grows at pH 10.5.

Highlights

ATP is the molecular currency for a living cell, which is merely growing and dividing and continuously responding to external environmental stimuli
Various studies based on the mechanism of proton binding[7,8], through hydronium ion proton retention and transportation for ATP synthesis in the bacterial system including alkaliphiles[9,10] suggest the presence of alkaliphile specific conserved amino acid motifs in transmembrane helix-4 (TMH-4) and TMH-5 of the a-subunit and the inner and the outer helix of the c-subunit[3,11,12,13,14] of the ATP synthase Fo subunit as well as Na+/H+ antiporter[15] and other cation binding proton transporters including multiple drug transporters[6,16]
This study explores the comparison of the ATP synthase a-subunit of facultative alkaliphilic aerobes isolated from Lonar Lake with established and reported alkaliphiles

Summary

Introduction

ATP is the molecular currency for a living cell, which is merely growing and dividing and continuously responding to external environmental stimuli. Various studies based on the mechanism of proton binding[7,8], through hydronium ion proton retention and transportation for ATP synthesis in the bacterial system including alkaliphiles[9,10] suggest the presence of alkaliphile specific conserved amino acid motifs in transmembrane helix-4 (TMH-4) and TMH-5 of the a-subunit and the inner and the outer helix of the c-subunit[3,11,12,13,14] of the ATP synthase Fo subunit as well as Na+/H+ antiporter[15] and other cation binding proton transporters including multiple drug transporters[6,16].

Results

Conclusion