Deamination role of inducible glutamate dehydrogenase isoenzyme 7 in Brassica napus leaf protoplasts

2011 ◽  
Vol 72 (7) ◽  
pp. 587-593 ◽  
Author(s):  
Masami Watanabe ◽  
Ohnishi Yumi ◽  
Yasuhiro Itoh ◽  
Kaori Yasuda ◽  
Kazunari Kamachi ◽  
...  
Keyword(s):  
Brassica Napus ◽  
Glutamate Dehydrogenase ◽  
Dehydrogenase Isoenzyme ◽  
Leaf Protoplasts

scholarly journals Apoptosis-like cell death of Brassica napus leaf protoplasts

2002 ◽  
Vol 156 (3) ◽  
pp. 417-426 ◽  
Author(s):  
Masami Watanabe ◽  
Daisuke Setoguchi ◽  
Koichi Uehara ◽  
Wakako Ohtsuka ◽  
Yukio Watanabe
Keyword(s):  
Cell Death ◽  
Brassica Napus ◽  
Leaf Protoplasts

Purification and characterization of two glutamate dehydrogenase isoenzymes from Brassica napus

1999 ◽  
Vol 37 (10) ◽  
pp. 731-739 ◽  
Author(s):  
Masami Watanabe ◽  
Toshihiko Hoshino ◽  
Atsushi Kikuchi ◽  
Yukio Watanabe
Keyword(s):  
Brassica Napus ◽  
Glutamate Dehydrogenase ◽  
Purification And Characterization

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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