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PLANT PHYSIOLOGY , Vol 113, Issue 2 575-586, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Growth and Photosynthesis under High and Low Irradiance of Arabidopsis thaliana Antisense Mutants with Reduced Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Content
N. A. Eckardt, G. W. Snyder, A. R. Portis Jr and W. L. Ogren
Department of Plant Biology, University of Illinois, Urbana, Illinois (N.A.E.)
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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