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Microbiology 152 (2006), 2727-2734; DOI  10.1099/mic.0.28942-0
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Microbiology 152 (2006), 2727-2734; DOI  10.1099/mic.0.28942-0
© 2006 Society for General Microbiology

Identification of the Mycobacterium tuberculosis GlnE promoter and its response to nitrogen availability

Carey A. Pashley, Amanda C. Brown, Dina Robertson and Tanya Parish

Centre for Infectious Disease, Institute for Cell and Molecular Science, Barts and the London, London E1 2AT, UK

Correspondence
Tanya Parish
t.parish{at}qmul.ac.uk

Adenylyltransferase, GlnE, has a predicted role in controlling the enzymic activity of glutamine synthetase, the key enzyme in ammonia assimilation. It was previously demonstrated that glnE is an essential gene in Mycobacterium tuberculosis. glnE is located downstream of glnA2, one of four glutamine synthetases. The expression of GlnE under various conditions was determined. Although a co-transcript of glnA2 and glnE was detectable, the major transcript was monocistronic. A transcriptional start site immediately upstream of glnE was identified and it was shown by site-directed mutagenesis that the predicted –10 region is a functional promoter. It was demonstrated that in a Mycobacterium smegmatis background M. tuberculosis PglnE was up-regulated in ammonia- or glutamine-containing media.


Abbreviations: GS, glutamine synthetase; RACE, rapid amplification of cDNA ends; RT-qPCR, quantitative RT-PCR




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P. Carroll, C. A. Pashley, and T. Parish
Functional Analysis of GlnE, an Essential Adenylyl Transferase in Mycobacterium tuberculosis
J. Bacteriol., July 15, 2008; 190(14): 4894 - 4902.
[Abstract] [Full Text] [PDF]




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