L-Methionine-SR-sulfoximine as a probe for the role of glutamine synthetase in nitrogenase switch-off by ammonia and glutamine in Rhodopseudomonas palustris

1983 ◽  
Vol 134 (1) ◽  
pp. 17-22 ◽  
Author(s):  
Daniel J. Arp ◽  
Walter G. Zumft
Keyword(s):  
Glutamine Synthetase ◽  
Rhodopseudomonas Palustris

scholarly journals The Overexpression of Glutamine Synthetase in Transgenic Poplar: A Review

2006 ◽  
Vol 55 (1-6) ◽  
pp. 278-284 ◽  
Author(s):  
E. G. Kirby ◽  
F. Gallardo ◽  
H. Man ◽  
R. El-Khatib
Keyword(s):  
Glutamine Synthetase ◽  
Woody Plant ◽  
Forest Tree ◽  
Considerable Effort ◽  
Physiological Mechanisms ◽  
Enhanced Resistance ◽  
Enhanced Expression ◽  
Use Efficiency

Abstract In investigating the pivotal role of glutamine synthetase in woody plant development, we have strived to develop an understanding of the biochemical and physiological mechanisms whereby enhanced expression of glutamine synthetase (GS) in poplar contributes to vegetative growth through enhanced nitrogen use efficiency. Considerable effort has also centered on characterization of enhanced resistance of transgenic GS overexpressor lines to abiotic stresses and proposed mechanisms. This summary of our work also focuses on future applications in forest tree improvement.

scholarly journals Role of the complex upstream region of the GDH2 gene in nitrogen regulation of the NAD-linked glutamate dehydrogenase in Saccharomyces cerevisiae.

1991 ◽  
Vol 11 (12) ◽  
pp. 6229-6247 ◽  
Author(s):  
S M Miller ◽  
B Magasanik
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Glutamine Synthetase ◽  
Nitrogen Source ◽  
Glutamate Dehydrogenase ◽  
Regulatory System ◽  
Sole Source ◽  
Lacz Fusion ◽  
Upstream Region ◽  
In Cells

We analyzed the upstream region of the GDH2 gene, which encodes the NAD-linked glutamate dehydrogenase in Saccharomyces cerevisiae, for elements important for the regulation of the gene by the nitrogen source. The levels of this enzyme are high in cells grown with glutamate as the sole source of nitrogen and low in cells grown with glutamine or ammonium. We found that this regulation occurs at the level of transcription and that a total of six sites are required to cause a CYC1-lacZ fusion to the GDH2 gene to be regulated in the same manner as the NAD-linked glutamate dehydrogenase. Two sites behaved as upstream activation sites (UASs). The remaining four sites were found to block the effects of the two UASs in such a way that the GDH2-CYC1-lacZ fusion was not expressed unless the cells containing it were grown under conditions favorable for the activity of both UASs. This complex regulatory system appears to account for the fact that GDH2 expression is exquisitely sensitive to glutamine, whereas the expression of GLN1, coding for glutamine synthetase, is not nearly as sensitive.

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