Plant Molecular Biology

, Volume 11, Issue 3, pp 335–344

Expression of the Escherichia coli glutamate dehydrogenase gene in the cyanobacterium Synechococcus PCC6301 causes ammonium tolerance

Authors

  • D. A Lightfoot
    • Department of GeneticsUniversity of Leeds
  • A. J. Baron
    • Department of GeneticsUniversity of Leeds
  • J. C. Wootton
    • Department of GeneticsUniversity of Leeds
Article

DOI: 10.1007/BF00027390

Cite this article as:
Lightfoot, D.A., Baron, A.J. & Wootton, J.C. Plant Mol Biol (1988) 11: 335. doi:10.1007/BF00027390

Abstract

The unicellular cyanobacterium Synechococcus PCC6301 lacks a hybridisable homologue of the strongly conserved gdhA gene of E. coli that encodes NADP-specific glutamate dehydrogenase. This is consistent with the failure to find this enzyme in extracts of the cyanobacterium. The E. coli gdhA gene was transferred to Synechococcus PCC6301 by transformation with an integrative vector. High levels of glutamate dehydrogenase activity, similar to those found in ammonium grown E. coli cells, were found in these transformants. These transformed cyanobacteria displayed an ammonium tolerant phenotype, consistent with the action of their acquired glutamate dehydrogenase activity as an ammonium detoxification mechanism. Minor differences in colony size and in growth at low light intensity were also observed.

Key words

ammonia assimilationammonia toxicitycyanobacteriaglutamatedehydrogenaseE. coli gdhA geneSynechococcus PCC6301
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Copyright information

© Kluwer Academic Publishers 1988