Archives of Microbiology

, Volume 120, Issue 3, pp 195–200 | Cite as

Alteration of cyanobacterial glutamine synthetase activity in vivo in response to light and NH 4 +

  • P. Rowell
  • M. J. A. M. Sampaio
  • J. K. Ladha
  • W. D. P. Stewart


Extractable glutamine synthetase activity of the cyanobacterium Anabaena cylindrica was reduced by approximately 50% when N2-fixing cultures were treated with 10 mM NH 4 + or were placed in darkness. The deactivated enzyme could be rapidly reactivated (within 5 min) by adding 40 mM 2-mercaptoethanol to the biosynthetic reaction mixture. The enzyme could also be reactivated in vivo by replacing the culture in light or by removing NH 4 + . When the enzyme was deactivated by simultaneously adding NH 4 + and placing the culture in darkness, reactivation occurred on reillumination and removal of NH 4 + . The removal of NH 4 + in darkness did not result in reactivation. On in vitro reactivation of glutamine synthetase from dark or NH 4 + -treated cultures the maximum glutamine synthetase activity observed frequently exceeded that of glutamine synthetase extracted from untreated cultures. Anacystis nidulans showed a similar type of reversible dark deactivation to A. cylindrica but Plectonema boryanum and a Nostoc did not. With A. cylindrica, a direct positive correlation between the size of the intracellular pool of glutamate and biosynthetic glutamine synthetase activity occurred during light/dark shifts, and on treatment with NH 4 + . The changes in activity of glutamine synthetase in A. cylindrica in response to light resemble in some respects the light modulation of enzymes of the oxidative and reductive pentose phosphate pathways noted in cyanobacteria by others.

Key words

Blue-green algae Cyanobacteria Glutamine synthetase Light-modulation Anabaena cylindrica NH4+-deactivation 


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Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • P. Rowell
    • 1
  • M. J. A. M. Sampaio
    • 1
  • J. K. Ladha
    • 1
  • W. D. P. Stewart
    • 1
  1. 1.Department of Biological SciencesUniversity of DundeeDundeeScotland

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