Association of ATP: glutamine synthetase adenylyltransferase activity with the PI component of the glutamine synthetase deadenylylation system.

  • Anderson W
  • Hennig S
  • Ginsburg A
 et al. 
  • 3


    Mendeley users who have this article in their library.
  • 27


    Citations of this article.


Regulation of glutamine synthetase (EC 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 P(I) protein) are inseparable by a variety of fractionation procedures. The adenylyltransferase and P(I)-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 P(I)-deadenylylation activity are associated with the same protein complex.

Author-supplied keywords

  • Adenine Nucleotides
  • Adenosine Triphosphatases
  • Adenosine Triphosphatases: isolation & purificatio
  • Bacterial Proteins
  • Bacterial Proteins: isolation & purification
  • Chromatography
  • Escherichia coli
  • Escherichia coli: enzymology
  • Gel
  • Glutamine
  • Ligases
  • Ligases: isolation & purification
  • Ligases: metabolism
  • Protein Denaturation
  • Transferases
  • Transferases: metabolism

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • W B Anderson

  • S B Hennig

  • A Ginsburg

  • E R Stadtman

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free