Rubisco activities, properties, and regulation in three different C4 grasses under drought

In C4 plants, water deficit may decrease photosynthetic CO2 assimilation independently of changes in stomatal conductance, suggesting decreased turnover by ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The activity and biochemistry of Rubisco was studied in three different C4 grasses: Paspalum dilatatum, Cynodon dactylon, and Zoysia japonica. The objectives were to characterize the C4 Rubisco in these species and to identify factors associated with decreased photosynthetic rates caused by drought. Rubisco isolated from each of the three C4 grasses was characterized by smaller specificity factors (SC/O), larger Michaelis–Menten constants for CO2 (Kc) and O2 (Ko), and larger maximum carboxylation velocities (Vc) than Rubisco from wheat, which can be rationalized in terms of the CO2-rich environment of C4 Rubisco in the bundle sheath. During leaf dehydration the quantity and maximum activity of Rubisco remained unchanged but the initial and total activities declined slightly, possibly due to increased inhibition. Tight-binding inhibitors were present in the light but were more abundant in the dark, especially in Z. japonica, and increased in quantity with drought stress. The inhibitor from darkened leaves of Z. japonica was identified as 2-carboxyarabinitol-1-phosphate (CA1P). Consistent with the presence of CA1P, the total activity of Rubisco was decreased after 12 h darkness in Z. japonica. Ribulose-1,5-bisphosphate (RuBP) in the leaves decreased with drought stress, to quantities approximating those of Rubisco catalytic sites. The magnitude of the decrease in RuBP suggested that, at least in C. dactylon and Z. japonica, it could contribute to the drought-induced decrease in photosynthesis

Finishing the euchromatic sequence of the human genome

The sequence of the human genome encodes the genetic instructions for human physiology, as well as rich information about human evolution. In 2001, the International Human Genome Sequencing Consortium reported a draft sequence of the euchromatic portion of the human genome. Since then, the international collaboration has worked to convert this draft into a genome sequence with high accuracy and nearly complete coverage. Here, we report the result of this finishing process. The current genome sequence (Build 35) contains 2.85 billion nucleotides interrupted by only 341 gaps. It covers ∼99% of the euchromatic genome and is accurate to an error rate of ∼1 event per 100,000 bases. Many of the remaining euchromatic gaps are associated with segmental duplications and will require focused work with new methods. The near-complete sequence, the first for a vertebrate, greatly improves the precision of biological analyses of the human genome including studies of gene number, birth and death. Notably, the human enome seems to encode only 20,000-25,000 protein-coding genes. The genome sequence reported here should serve as a firm foundation for biomedical research in the decades ahead

Temperature Dependence of the Enzymic Carboxylation and Oxygenation of Ribulose 1,5-Bisphosphate in Relation to Effects of Temperature on Photosynthesis

Carboxylase and oxygenase activities of ribulose bisphosphate carboxylase purified from wheat were measured over the temperature range 5 to 35°C either at constant O(2) and CO(2) concentrations or where the O(2) and CO(2) simulated the concentrations in water equilibrated at each temperature with the same gaseous phase. At constant CO(2) (14 micromolar) and O(2) (0.34 millimolar), the oxygenase to carboxylase ratio remained constant at 0.21 between 5 and 25°C but increased to 0.26 at 35°C. At O(2) and CO(2) concentrations near those expected in water equilibrated with air (21% [v/v] O(2)) containing 300 μl/l CO(2) at the various temperatures, the ratio of oxygenase to carboxylase activity increased 2.2-fold between 15 and 35°C. At CO(2) and O(2) concentrations expected in water in equilibrium with subatmospheric concentrations of CO(2) in air (21% [v/v] O(2), 210 μl/l CO(2)), the oxygenase to carboxylase ratio increased from 0.25 at 10°C to 0.56 at 35°C. Between 20 and 30°C, the apparent Q(10) value for the oxygenase reaction was 1.78 and that for the carboxylase was 1.26. Hence, the different responses of photosynthesis and photorespiration to temperature are due more to changes in the relative solubilities of CO(2) and O(2) (the solubility ratio) than to changes in kinetic parameters of the reactions catalyzed by ribulose bisphosphate carboxylase

Using Simulations to Teach International Issues: An Analysis of the Multinational Management Game’s Learning Environment

The panel discussion will conclude with a descriptive view of the Multinational Management Game’s “shell” and administrative characteristics

Comparison of the specific activity of ribulose‐1,5‐bis‐phosphate carboxylase‐oxygenase from some C3 and C4 plants

The specific activity of ribulose‐1,5‐bisphosphate carboxylase‐oxygenase (Rubisco, EC 4.1.1.39) was measured from the crude extracts of five C3 plants consisting of wheat (Triticum aestivum L. cv. Maris Mink), spinach (Spinacia oleracea L.), pea (Pisum sativum L. cv. Greenfeast), pumpkin (Cucurbita pepo L. cv. Jättiläismeloni) and Ceratodon purpureus (Hedw.) Brid., and two C4 plants, maize (Zea mays L. ETA F1) and sugar sorghum [Sorghum saccharatum (L. emend, L.) Moench]. The amount of Rubisco in the crude extracts was estimated by polyacrylamide gel electro‐phoresis with the Coomassie Brilliant Blue staining procedure. The amounts of the dye bound to the purified Rubisco of different higher plants were similar. The method gave a linear response for both purified enzyme and crude extracts, and the results agreed with those observed by immunochemical methods. The addition of positive effectors such as inorganic phosphate was necessary to obtain maximal activity in the crude extracts of all the studied plants except in that of maize. No significant differences in the specific carboxylase activity at 25°C were found between the C3 and C4 plants