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Glutamine synthetase in ribulose 1,5-bisphosphate carboxylase/oxygenase deficient tobacco mutants in cell suspension culture

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Abstract

In two tobacco mutants lacking ribulose, 1,5-bisphosphate carboxylase/oxygenase the amount of glutamine synthetase and its activity were determined and compared with the wild type green cells. It was shown that in these two mutants glutamine synthetase protein content was six times lower than in the wild type. This situation was comparable to that found in etiolated cells where ribulose 1,5-bisphosphate carboxylase/oxygenase was absent. These observations suggest that a common regulatory mechanism might control the dual light dependent biosynthesis of both enzymes. The results have also implications concerning the efficiency of the reassimilation of ammonia by chloroplastic glutamine synthetase during the photorespiratory process.

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Abbreviations

GS:

Glutamine synthetase

RuBisCo:

Ribulose 1,5-bisphosphate carboxylase/oxygenase

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Authors and Affiliations

  1. Physiologie Végétale Métabolique E. R. A. CNRS, Université de Paris-Sud, no 799 Bâtiment 430, 91405, Orsay Cedex, France

    Bertrand Hirel

  2. Structure et Métabolisme des Plantes, L. A. au CNRS, Université de Paris-Sud, no 40 Bâtiment 430, 91405, Orsay Cedex, France

    Aimé Nato

  3. Microbiologie Forestière, Institut National de la Recherche Agronomique, C.N.R.F. de Champenoux, 54280, Seichamps, France

    Francis Martin

Authors
  1. Bertrand Hirel
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  2. Aimé Nato
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  3. Francis Martin
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Communicated by W. Barz

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Hirel, B., Nato, A. & Martin, F. Glutamine synthetase in ribulose 1,5-bisphosphate carboxylase/oxygenase deficient tobacco mutants in cell suspension culture. Plant Cell Reports 3, 106–108 (1984). https://doi.org/10.1007/BF02441011

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  • DOI: https://doi.org/10.1007/BF02441011

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