Abstract:
BACKGROUND:Although the gene encoding for glutamine synthetase (glnA) 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 (glnA1) is essential for growth in M. tuberculosis, while the other copies (glnA2, glnA3 and glnA4) are not. RESULTS:In this report it is shown that the glnA1 and glnA2 encoded glutamine synthetase sequences were inherited from an Actinobacteria ancestor, while the glnA4 and glnA3 encoded GS sequences were sequentially acquired during Actinobacteria speciation. The glutamine synthetase sequences encoded by glnA4 and glnA3 are undergoing reductive evolution in the mycobacteria, whilst those encoded by glnA1 and glnA2 are more conserved. CONCLUSION:Different selective pressures by the ecological niche that the organisms occupy may influence the sequence evolution of glnA1 and glnA2 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.
journal_name
BMC Evol Bioljournal_title
BMC evolutionary biologyauthors
Hayward D,van Helden PD,Wiid IJdoi
10.1186/1471-2148-9-48subject
Has Abstractpub_date
2009-02-26 00:00:00pages
48issn
1471-2148pii
1471-2148-9-48journal_volume
9pub_type
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journal_title:BMC evolutionary biology
pub_type: 杂志文章
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更新日期:2009-08-28 00:00:00
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