Regulation of Glutamine Synthetase Degradation

  • C. N. Oliver
  • R. L. Levine
  • E. R. Stadtman
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)


There is considerable evidence that the synthesis and degradation of proteins is a dynamic process which governs the steady-state level of enzymes in the cell. Although a great deal is known about the factors that regulate the rates of enzyme synthesis, relatively little is known about the mechanism involved in the regulation of enzyme degradation. It is known that various enzymes are degraded at different rates which are determined in part by undefined nutritional factors and that degradation is dependent upon a supply of metabolic energy (ATP) (Goldberg and St. John 1976; Holzer and Heinrich 1980). To gain more insight in to this problem, studies in our laboratory (Fulks 1977; Maurizi 1980; Oliver and Stadtman 1980) have been directed toward the development of cell-free enzyme preparations that catalyze the selective proteolysis of individual enzymes.


Glutamine Synthetase Glutamine Synthetase Activity Mixed Function Oxidase Mixed Function Oxidase System Inactivation System 
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  1. Beers RF, Jr, Sizer IW (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195: 133–140.PubMedGoogle Scholar
  2. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254.PubMedCrossRefGoogle Scholar
  3. Fulks RM (1977) Regulation of glutamine synthetase degradation in Klebsiella aerogenes. Fed Proc (Abstr) 36: 919.Google Scholar
  4. Goldberg AL, St John AC (1976) Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem 45: 747–803.PubMedCrossRefGoogle Scholar
  5. Hassan HM, Fridovich I (1978) Regulation of the synthesis of catalase and peroxidase in Escherichia coli. J Biol Chem 253: 6445–6450.PubMedGoogle Scholar
  6. Holzer H, Heinrich PC (1980) Control of proteolysis. Annu Rev Biochem 49: 63–91.PubMedCrossRefGoogle Scholar
  7. Levine RL, Oliver CN, Fulks RM, Stadtman ER (to be published 1981) Turnover of bacterial glutamine synthetase: Proteolysis is preceded by oxidative inactivation. Proc Natl Acad Sci USAGoogle Scholar
  8. Maurizi MR (1980) Degradation of specific enzymes in Escherichia coli. Fed Proc (Abstr) 39: 403.Google Scholar
  9. Oliver CN, Stadtman ER (1980) Inactivation and proteolysis of glutamine synthetase by Escherichia coli extracts. Fed Proc (Abstr) 39: 402.Google Scholar
  10. Oliver CN, Levine RL, Stadtman ER (to be published 1981) Regulation of glutamine synthetase degradation. In: Ornston LN (ed) Experiences in biochemical perception. Academic Press, London New York.Google Scholar
  11. Sasarman A, Surcleanu M, Sźegli G, Horodniceanu T, Greceanu V, Dumitrescu A (1968) Hemin-deficient mutants of Escherichia coli K-12. J Bacteriol 96: 570–572.PubMedGoogle Scholar
  12. Stadtman ER, Davis JN, Smyrniotis PZ, Wittenberger ME (1979) Enzymatic procedures for determining the average state of adenylylation of Escherichia coli glutamine synthetase. Anal Biochem 95: 275–285.PubMedCrossRefGoogle Scholar
  13. Tsaftaris AS, Sorenson JC, Scandalios JG (1980) Glycosylation of catalase inhibitor necessary for activity. Biochem Biophys Res Commun 92: 889–895.PubMedCrossRefGoogle Scholar
  14. Udenfriend S, Clark CT, Axelrod J, Brodie BB (1954) Ascorbic acid in aromatic hydroxylation. I. A model system for aromatic hydroxylation. J Biol Chem 208: 731–739.Google Scholar

Copyright information

© Springer-Verlag, Berlin Heidelberg 1981

Authors and Affiliations

  • C. N. Oliver
    • 1
  • R. L. Levine
    • 1
  • E. R. Stadtman
    • 1
  1. 1.Laboratory of BiochemistryNational Heart, Lung, and Blood Institute, National Institutes of HealthBethesdaUSA

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