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Background  Although the gene encoding for glutamine synthetase ( gln A) is essential in several organisms, multiple glnA copies have been identified in bacterial genomes such as those of the phylum  Actinobacteria , notably the mycobacterial species. Intriguingly, previous reports have shown that only one copy ( gln A1) is essential for growth in  M. tuberculosis , while the other copies ( gln A2,  gln A3 and  gln A4) are not.    Results  In this report it is shown that the  gln A1 and  gln A2 encoded glutamine synthetase sequences were inherited from an  Actinobacteria  ancestor, while the  gln A4 and  gln A3 encoded GS sequences were sequentially acquired during  Actinobacteria  speciation. The glutamine synthetase sequences encoded by  gln A4 and  gln A3 are undergoing reductive evolution in the mycobacteria, whilst those encoded by  gln A1 and  gln A2 are more conserved.    Conclusion  Different selective pressures by the ecological niche that the organisms occupy may influence the sequence evolution of  gln A1 and  gln A2 and thereby affecting phylogenies based on the protein sequences they encode. The findings in this report may impact the use of similar sequences as molecular markers, as well as shed some light on the evolution of glutamine synthetase in the mycobacteria.

Glutamine synthetase sequence evolution in the mycobacteria and their use as molecular markers for Actinobacteria speciation