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Title: Regulation of pyruvate orthophosphate dikinase gene expression in C/sub 3/ plants as compared to that in C/sub 4/ plants

Thesis/Dissertation ·
OSTI ID:6025901

Pyruvate orthophosphate dikinase (PPDK) was found to be more widely distributed in both leaves and seeds of C/sub 3/ and C/sub 4/ plants than previously realized. Physicochemical and enzymic properties appear to be strongly conserved over this distribution. In wheat, a C/sub 3/ plant, both in seeds and leaves, the amount of PPDK protein is developmentally regulated. In seeds the enzyme level is determined by the level of PPDK mRNA. The role of PPDK seems to be providing phosphoenolpyruvate as a substrate for amino acid interconversions during development. In leaves, the PPDK protein level increased with development. PPDK is present in chloroplasts also in C/sub 3/ plants. In maize, a C/sub 4/ plant, PPDK is not limited to mesophyll cells but also is present in bundle sheath cells, kernels and other tissues. In the leaf, the appearance and accumulation of PPDK is well coordinated with other enzymes of carbon metabolism. In maize callus, a heterotrophic type PPDK is synthesized independently in light and is active in the dark. Shoot formation and establishment of autotrophy enhances the accumulation of the leaf-type PPDK and leaf-type isozymes of phosphoenolpyruvate carboxylase and NADP-malic enzyme. Ultrastructural changes and /sup 14/C uptake patterns during regeneration of leaves from callus indicate that cell differentiation and Kranz anatomy are essential for the functional C/sub 4/ photosynthesis as well as for coordinated expression of enzymes involved in the C/sub 4/ pathway.

Research Organization:
California Univ., Berkeley (USA)
OSTI ID:
6025901
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English