Growth and Photosynthesis under High and Low Irradiance of Arabidopsis thaliana Antisense Mutants with Reduced Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Content (original) (raw)

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Department of Plant Biology, University of Illinois, Urbana, Illinois (N.A.E.)

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Department of Plant Biology, University of Illinois, Urbana, Illinois (N.A.E.)

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Department of Plant Biology, University of Illinois, Urbana, Illinois (N.A.E.)

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Department of Plant Biology, University of Illinois, Urbana, Illinois (N.A.E.)

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Published:

01 February 1997

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N. A. Eckardt, G. W. Snyder, A. R. Portis Jr, W. L. Ogren, Growth and Photosynthesis under High and Low Irradiance of Arabidopsis thaliana Antisense Mutants with Reduced Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Content, Plant Physiology, Volume 113, Issue 2, February 1997, Pages 575–586, https://doi.org/10.1104/pp.113.2.575
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Abstract

Photosynthesis and growth to maturity of antisense ribulose-1,5- bisphosphate carboxylase/oxygenase (Rubisco) activase Arabidopsis thaliana with reduced concentrations of activase relative to wild-type (Wt) plants were measured under low (200 [mu]mol m-2 s-1) and high (600 [mu]mol m-2 s-1) photosynthetic photon flux density growing conditions. Both growth and photosynthesis were significantly reduced in an Arabidopsis clone (R100) with 30 to 40% Wt activase, an effect that was more pronounced in high light. The aboveground biomass of the antisense clone R100 reached 80% of Wt under low light and 65% of Wt under high light. Decreased growth in the antisense plants was attributed to reduced relative rates of growth and leaf area expansion early in development; all plants attained similar values of relative rates of growth and leaf elongation by 21 d after planting. Reductions in photosynthesis were attributed to decreased Rubisco activation in the antisense plants. Rubisco constituted about 40% of total soluble protein in both Wt and clone R100 under both light regimes. Activase content was 5% and 1.4% of total soluble protein in Wt and clone R100, respectively, and also was unaffected by growth irradiance. The stoichiometry of Rubisco to activase was estimated at 20 Rubisco active sites per activase tetramer in Wt Arabidopsis and 60 to 80 in the transgenic clone R100. We conclude that Wt Arabidopsis does not contain Rubisco activase in great excess of the amount required for optimal growth.

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Copyright © 1997 by American Society of Plant Biologists

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