CARBON METABOLISM ENZYMES AND PHOTOSYNTHESIS IN TRANSGENIC TOBACCO (NICOTIANA-TABACUM-L) HAVING EXCESS PHYTOCHROME

J.M. Keller et al. (1989, EMBO J. 8, 1005-1012) introduced a phytochrome gene controlled by a cauliflower mosaic virus 35S promoter into tobacco (Nicotiana tabacum L.) providing material to test whether several photosynthesis enzymes can be increased by one modification to the plant. We report here that this transgenic tobacco had greater amounts of all enzymes examined as well as greater amounts of total protein and chlorophyll per unit leaf area. Fructose bisphosphatase (E.C. 3.1.3.11), glyceraldehyde 3-phosphate dehydrogenase (E.C. 1.2.1.12), and sucrose-phosphate synthase (E.C. 2.4.1.14) were also higher when expressed per unit protein. However, ribulose-1,5-bisphosphate carboxylase (E.C. 4.1.1.39) amount per unit leaf protein was the same in transgenic and wild-type (WT) plants. Photosynthesis in the transgenic plants was lower than in WT at air levels of CO2, but higher than in WT above 1000-mu-bar CO2. The photosynthesis results indicated a high resistance to CO2 diffusion in the mesophyll of the transgenic plants. Examination of electron micrographs showed that chloroplasts in the transgenic plants were often cup-shaped, preventing close association between chloroplast and cell surface. Chloroplast cupping may have caused the increase in the mesophyll resistance to CO2 diffusion. We conclude that it is possible to affect more than one enzyme with a single modification, but unexpected physical modifications worsened the photosynthetic performance of this plant.