Regulation of glutamine synthetase from Saccharomyces cerevisiae by repression, inactivation and proteolysis.

Abstract

Glutamine synthetase activity is modulated by nitrogen repression and by two distinct inactivation processes. Addition of glutamine to exponentially grown yeast leads to enzyme inactivation. 50% of glutamine synthetase activity is lost after 30 min (a quarter of the generation time). Removing glutamine from the growth medium results in a rapid recovery of enzyme activity. A regulatory mutation (gdhCR mutation) suppresses this inactivation by glutamine in addition to its derepressing effect on enzymes involved in nitrogen catabolism. The gdhCR mutation also increases the level of proteinase B in exponentially grown yeast. Inactivation of glutamine synthetase is also observed during nitrogen starvation. This inactivation is irreversible and consists very probably of a proteolytic degradation. Indeed, strains bearing proteinase A, B and C mutations are no longer inactivated under nitrogen starvation.

• Authors: C Legrain, S Vissers, E Dubois, M Legrain, J M Wiame
• Journal: European journal of biochemistry (Eur J Biochem) Vol. 123 Issue 3 Pg. 611-6 (Apr 1982) ISSN: 0014-2956 [Print] England
• PMID: 6122575 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Glutamate-Ammonia Ligase
• Nitrogen

Topics

• Glutamate-Ammonia Ligase (antagonists & inhibitors, genetics, physiology)
• Mutation
• Nitrogen (pharmacology)
• Saccharomyces cerevisiae (enzymology)