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Immunolocalization of Rubisco Activase and Rubisco in C3 and C4 Plant Tissues

Published online by Cambridge University Press:  02 July 2020

S. Madhavan
Affiliation:
Department of Biochemistry, University of Nebraska, Lincoln, NE, 68588-0664
M. S. Miller-Goodman
Affiliation:
Department of Agronomy & Soils, Auburn University, AL, 36849-5412
K. W. Lee
Affiliation:
School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE, 68588-0118
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Extract

Ribulose bisphosphate carboxylase/oxygenase (Rubisco), an abundant enzyme in chloroplasts, must be activated by CO2 in order for it to catalyze the carboxylation of ribulose bisphosphate. Rubisco activase, a nuclear encoded chloroplast protein was first identified as a biochemical lesion in the rca mutant of Arabidopsis (1) which lacked this enzyme. Study of Rubisco in this mutant (2) and transgenic tobacco plants with reduced Rubisco activase levels showed that Rubisco could not achieve and maintain an adequate level of activity, in vivo, without an activase. Rubisco activase promotes ‘activation’ of Rubisco by overcoming the deleterious effects of tight binding sugar phosphates and low chloroplast CO2 levels on catalysis and carbamylation (1).

Rubisco activase has been detected in higher plants (3), in unicellular green algae (4,5) and in cyanobacteria (6). Though the presence of Rubisco in guard cell chlroplasts was a subject of controversy, several immunolight and immunoelectron microscopic studies have demonstrated the presence of Rubisco in guard cells (7).

Type
Biological Specimen Preparation/Cytochemistry/ Immunolabeling/Immunocytochemistry
Copyright
Copyright © Microscopy Society of America

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References

References:

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