Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Nov;67(3):1417–1424. doi: 10.1073/pnas.67.3.1417

Association of ATP: Glutamine Synthetase Adenylyltransferase Activity with the PI Component of the Glutamine Synthetase Deadenylylation System

Wayne B Anderson 1,*, S Barbara Hennig 1, Ann Ginsburg 1, E R Stadtman 1
PMCID: PMC283368  PMID: 4249662

Abstract

Regulation of glutamine synthetase (EC 6.3.1.2) in Escherichia coli is mediated by adenylylation and deadenylylation of the enzyme. The present studies show that one protein is a common component of both the adenylylation and deadenylylation systems. Thus, the ATP:glutamine synthetase adenylyltransferase, which catalyzes adenylylation of glutamine synthetase, and one of the two proteins required for deadenylylation (the PI protein) are inseparable by a variety of fractionation procedures. The adenylyltransferase and PI-deadenylylating activities behave as a single protein upon filtration through Agarose A 0.5 gel, and during chromatography on DE32 cellulose and hydroxyapatite columns. They migrate as a single protein band during electrophoresis on polyacrylamide gel and have identical susceptibilities to heat inactivation. These data indicate that the adenylyltransferase and the PI-deadenylylation activity are associated with the same protein complex.

Full text

PDF
1417

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Denton M. D., Ginsburg A. Conformational changes in glutamine synthetase from Escherichia coli. I. The binding of Mn2+ in relation to some aspects of the enzyme structure and activity. Biochemistry. 1969 Apr;8(4):1714–1725. doi: 10.1021/bi00832a055. [DOI] [PubMed] [Google Scholar]
  2. Ginsburg A., Yeh J., Hennig S. B., Denton M. D. Some effects of adenylylation on the biosynthetic properties of the glutamine synthetase from Escherichia coli. Biochemistry. 1970 Feb 3;9(3):633–649. doi: 10.1021/bi00805a025. [DOI] [PubMed] [Google Scholar]
  3. Kingdon H. S., Shapiro B. M., Stadtman E. R. Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1703–1710. doi: 10.1073/pnas.58.4.1703. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Kingdon H. S., Stadtman E. R. Regulation of glutamine synthetase. X. Effect of growth conditions on the susceptibility of Escherichia coli glutamine synthetase to feedback inhibition. J Bacteriol. 1967 Oct;94(4):949–957. doi: 10.1128/jb.94.4.949-957.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  6. Maizel J. V., Jr Acrylamide-gel electrophorograms by mechanical fractionation: radioactive adenovirus proteins. Science. 1966 Feb 25;151(3713):988–990. doi: 10.1126/science.151.3713.988. [DOI] [PubMed] [Google Scholar]
  7. Mantel M., Holzer H. Reversibility of the ATP:glutamine synthetase adenylyltransferase reaction. Proc Natl Acad Sci U S A. 1970 Mar;65(3):660–667. doi: 10.1073/pnas.65.3.660. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Mecke D., Wulff K., Liess K., Holzer H. Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli. Biochem Biophys Res Commun. 1966 Aug 12;24(3):452–458. doi: 10.1016/0006-291x(66)90182-3. [DOI] [PubMed] [Google Scholar]
  9. Shapiro B. M., Stadtman E. R. Glutamine synthetase deadenylylating enzyme. Biochem Biophys Res Commun. 1968 Jan 11;30(1):32–37. doi: 10.1016/0006-291x(68)90708-0. [DOI] [PubMed] [Google Scholar]
  10. Shapiro B. M. The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements. Biochemistry. 1969 Feb;8(2):659–670. doi: 10.1021/bi00830a030. [DOI] [PubMed] [Google Scholar]
  11. Woolfolk C. A., Shapiro B., Stadtman E. R. Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli. Arch Biochem Biophys. 1966 Sep 26;116(1):177–192. doi: 10.1016/0003-9861(66)90026-9. [DOI] [PubMed] [Google Scholar]
  12. Wulff K., Mecke D., Holzer H. Mechanism of the enzymatic inactivation of glutamine synthetase from E. coli. Biochem Biophys Res Commun. 1967 Sep 7;28(5):740–745. doi: 10.1016/0006-291x(67)90378-6. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES