Nitrogen metabolite repression of arginase, ornithine transaminase and allantoinase in a conditional ethionine-resistant mutant of Saccharomyces cerevisiae with low activity of catabolic NAD-specific glutamate dehydrogenase

1982 ◽  
Vol 48 (5) ◽  
pp. 417-432 ◽  
Author(s):  
W. J. Middelhoven ◽  
Mieke C. Hoogkamer-te Niet
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Glutamate Dehydrogenase ◽  
Resistant Mutant ◽  
Nitrogen Metabolite Repression ◽  
Ornithine Transaminase ◽  
Low Activity

Regulation of glutamine-repressible gene products by the GLN3 function in Saccharomyces cerevisiae

1984 ◽  
Vol 4 (12) ◽  
pp. 2758-2766
Author(s):  
A P Mitchell ◽  
B Magasanik
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Glutamine Synthetase ◽  
Glutamate Dehydrogenase ◽  
Opposite Effect ◽  
Nuclear Gene ◽  
Yeast Saccharomyces Cerevisiae ◽  
Two Dimensional Gel Electrophoresis ◽  
Regulatory Circuit ◽  
Glutamate Dehydrogenase Activity ◽  
Glutamine Limitation

Mutants of the yeast Saccharomyces cerevisiae have been isolated which fail to derepress glutamine synthetase upon glutamine limitation. The mutations define a single nuclear gene, GLN3, which is located on chromosome 5 near HOM3 and HIS1 and is unlinked to the structural gene for glutamine synthetase, GLN1. The three gln3 mutations are recessive, and one is amber suppressible, indicating that the GLN3 product is a positive regulator of glutamine synthetase expression. Four polypeptides, in addition to the glutamine synthetase subunit are synthesized at elevated rates when GLN3+ cultures are shifted from glutamine to glutamate media as determined by pulse-labeling and one- and two-dimensional gel electrophoresis. The response of all four proteins is blocked by gln3 mutations. In addition, the elevated NAD-dependent glutamate dehydrogenase activity normally found in glutamate-grown cells is not found in gln3 mutants. Glutamine limitation of gln1 structural mutants has the opposite effect, causing elevated levels of NAD-dependent glutamate dehydrogenase even in the presence of ammonia. We suggest that there is a regulatory circuit that responds to glutamine availability through the GLN3 product.

scholarly journals Improved Leavening Ability of a Wild Yeast, Saccharomyces cerevisiae AK46 2-deoxyglucose Resistant Mutant

2015 ◽  
Vol 21 (4) ◽  
pp. 623-630 ◽  
Author(s):  
Dai Mikumo ◽  
Masahiro Takaya ◽  
Yoshitake Orikasa ◽  
Takuji Ohwada
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Resistant Mutant ◽  
Wild Yeast ◽  
Leavening Ability

Isolation and characterization of an uncoupler-resistant mutant of Saccharomyces cerevisiae

1984 ◽  
Vol 8 (7) ◽  
pp. 507-516 ◽  
Author(s):  
Charles-Henri Dupont ◽  
Roland Caubet ◽  
Jean-Pierre Mazat ◽  
Bernard Guerin
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Resistant Mutant ◽  
Isolation 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.

Sign in / Sign up

Export Citation Format

Share Document