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PLANT PHYSIOLOGY , Vol 115, Issue 4 1681-1689, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Regulation and Localization of Key Enzymes during the Induction of Kranz-Less, C4-Type Photosynthesis in Hydrilla verticillata
N. C. Magnin, B. A. Cooley, J. B. Reiskind and G. Bowes
Department of Botany and the Center for Aquatic Plants, University of Florida, Gainesville, Florida 32611
Kranz-less, C4-type photosynthesis was induced in the submersed monocot
Hydrilla verticillata (L.f.) Royle. During a 12-d induction period the CO2
compensation point and O2 inhibition of photosynthesis declined linearly.
Phosphoenolpyruvate carboxylase (PEPC) activity increased 16-fold, with the
major increase occurring within 3 d. Asparagine and alanine
aminotransferases were also induced rapidly. Pyruvate orthophosphate
dikinase (PPDK) and NADP-malic enzyme (ME) activities increased 10-fold but
slowly over 15 d. Total ribulose-1,5-bisphosphate carboxylase/oxygenase
activity did not increase, and its activation declined from 82 to 50%.
Western blots for PEPC, PPDK, and NADP-ME indicated that increased protein
levels were involved in their induction. The H. verticillata NADP-ME
polypeptide was larger (90 kD) than the maize C4 enzyme (62 kD). PEPC and
PPDK exhibited up-regulation in the light. Subcellular fractionation of
C4-type leaves showed that PEPC was cytosolic, whereas PPDK and NADP-ME
were located in the chloroplasts. The O2 inhibition of photosynthesis was
doubled when C4-type but not C3-type leaves were exposed to diethyl
oxalacetate, a PEPC inhibitor. The data are consistent with a C4-cycle
concentrating CO2 in H. verticillata chloroplasts and indicate that Kranz
anatomy is not obligatory for C4-type photosynthesis. H. verticillata
predates modern terrestrial C4 monocots; therefore, this inducible
CO2-concentrating mechanism may represent an ancient form of C4
photosynthesis.
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