Interaction of Chloroplast and Nuclear Genomes in Regulating RuBP Carboxylase Activity

  • S. D. Kung
  • P. R. Rhodes
Part of the Basic Life Sciences book series (BLSC, volume 11)


Extensive studies of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase have provided much information on its structure, function, biosynthesis, mode of inheritance, and genetic variability (1-3). RuBP carboxylase, which in higher plants has been termed Fraction I protein, is found in all photosynthetic organisms as an oligomeric protein of high molecular weight (1-4). It catalyzes the carboxylation of RuBP, producing two molecules of glycerate 3-phosphate (PGA), the primary product of photosynthesis (3). In the presence of molecular oxygen, RuBP carboxylase can also catalyze the oxidation of RuBP, forming PGA and phosphoglycolate, which can be converted to glycolate, the substrate for photorespiration (3, 5). Since the balance between photosynthetic and photorespiratory processes determines a plant’s maximum yield, the ability of RuBP carboxylase to participate in either process has generated renewed interest in this enzyme.


Large Subunit Small Subunit Chloroplast Genome Nuclear Genome Male Sterile Line 
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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • S. D. Kung
    • 1
  • P. R. Rhodes
    • 1
  1. 1.Department of Biological SciencesUniversity of Maryland Baltimore CountyCatonsvilleUSA

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