NADP-MALATE DEHYDROGENASE IN THE C-4 PLANT FLAVERIA-BIDENTIS - COSENSE SUPPRESSION OF ACTIVITY IN MESOPHYLL AND BUNDLE-SHEATH CELLS AND CONSEQUENCES FOR PHOTOSYNTHESIS
Sj. Trevanion et al., NADP-MALATE DEHYDROGENASE IN THE C-4 PLANT FLAVERIA-BIDENTIS - COSENSE SUPPRESSION OF ACTIVITY IN MESOPHYLL AND BUNDLE-SHEATH CELLS AND CONSEQUENCES FOR PHOTOSYNTHESIS, Plant physiology, 113(4), 1997, pp. 1153-1165
Flaveria bidentis, a C-4 dicot, was transformed with sorghum (a monoco
t) cDNA clones encoding NADP-malate dehydrogenase (NADP-MDH; EC 1.1.1.
82) driven by the cauliflower mosaic virus 35S promoter. Although thes
e constructs were designed for overexpression, many transformants cont
ained between 5 and 50% of normal NADP-MDH activity, presumably by cos
ense suppression of the native gene. The activities of a range of othe
r photosynthetic enzymes were unaffected. Rates of photosynthesis in p
lants with less than about 10% of normal activity were reduced at high
light and at high [CO2], but were unaffected at low light or at [CO2]
below about 150 mu L L-1. The large decrease in maximum activity of N
ADP-MDH was accompanied by an increase in the activation state of the
enzyme. However, the activation state was unaffected in plants with 50
% of normal activity. Metabolic flux control analysis of plants with a
range of activities demonstrates that this enzyme is not important in
regulating the steady-state flux through C-4 photosynthesis in F. bid
entis. Cosense suppression of gene expression was similarly effective
in both the mesophyll and bundle-sheath cells. Photosynthesis of plant
s with very low activity of NADP-MDH in the bundle-sheath cells was on
ly slightly inhibited, suggesting that the presence of the enzyme in t
his compartment is not essential for supporting maximum rates of photo
synthesis.